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Serine/threonine-protein kinase 25 (EC 2.7.11.1) (Ste20-like kinase) (Sterile 20/oxidant stress-response kinase 1) (SOK-1) (Ste20/oxidant stress response kinase 1)

 STK25_HUMAN             Reviewed;         426 AA.
O00506; A8K6Z3; A8K7D2; B7Z9K1; Q15522; Q5BJF1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
27-SEP-2017, entry version 179.
RecName: Full=Serine/threonine-protein kinase 25;
EC=2.7.11.1;
AltName: Full=Ste20-like kinase;
AltName: Full=Sterile 20/oxidant stress-response kinase 1;
Short=SOK-1;
Short=Ste20/oxidant stress response kinase 1;
Name=STK25; Synonyms=SOK1, YSK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8887545;
Pombo C.M., Bonventre J.V., Molnar A., Kyriakis J., Force T.;
"Activation of a human Ste20-like kinase by oxidant stress defines a
novel stress response pathway.";
EMBO J. 15:4537-4546(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9160885; DOI=10.1038/sj.onc.1201043;
Osada S., Izawa M., Saito R., Mizuno K., Suzuki A., Hirai S., Ohno S.;
"YSK1, a novel mammalian protein kinase structurally related to Ste20
and SPS1, but is not involved in the known MAPK pathways.";
Oncogene 14:2047-2057(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis, and Uterus;
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).
[9]
FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-174, SUBCELLULAR
LOCATION, INTERACTION WITH GOLGA2, AND MUTAGENESIS OF LYS-49 AND
ASP-158.
PubMed=15037601; DOI=10.1083/jcb.200310061;
Preisinger C., Short B., De Corte V., Bruyneel E., Haas A.,
Kopajtich R., Gettemans J., Barr F.A.;
"YSK1 is activated by the Golgi matrix protein GM130 and plays a role
in cell migration through its substrate 14-3-3zeta.";
J. Cell Biol. 164:1009-1020(2004).
[10]
INTERACTION WITH CTTNBP2NL.
PubMed=18782753; DOI=10.1074/mcp.M800266-MCP200;
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
Aebersold R., Raught B., Gingras A.C.;
"A PP2A phosphatase high density interaction network identifies a
novel striatin-interacting phosphatase and kinase complex linked to
the cerebral cavernous malformation 3 (CCM3) protein.";
Mol. Cell. Proteomics 8:157-171(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Oxidant stress-activated serine/threonine kinase that
may play a role in the response to environmental stress. Targets
to the Golgi apparatus where it appears to regulate protein
transport events, cell adhesion, and polarity complexes important
for cell migration. {ECO:0000269|PubMed:15037601}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Interaction with Golgi matrix protein GOLGA2
leads to autophosphorylation on Thr-174, possibly as a consequence
of stabilization of dimer formation. The C-terminal non-catalytic
region inhibits the kinase activity.
{ECO:0000269|PubMed:15037601}.
-!- SUBUNIT: Homodimer. Interacts with CTTNBP2NL.
{ECO:0000269|PubMed:15037601, ECO:0000269|PubMed:18782753}.
-!- INTERACTION:
Q9Y376:CAB39; NbExp=3; IntAct=EBI-618295, EBI-306905;
Q8IYA8:CCDC36; NbExp=3; IntAct=EBI-618295, EBI-8638439;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-618295, EBI-739624;
Q08379:GOLGA2; NbExp=10; IntAct=EBI-618295, EBI-618309;
Q62839:Golga2 (xeno); NbExp=2; IntAct=EBI-618295, EBI-618335;
Q9BUL8:PDCD10; NbExp=18; IntAct=EBI-618295, EBI-740195;
Q9Y6E0:STK24; NbExp=4; IntAct=EBI-618295, EBI-740175;
O43815:STRN; NbExp=3; IntAct=EBI-618295, EBI-1046642;
P14373:TRIM27; NbExp=3; IntAct=EBI-618295, EBI-719493;
P63104:YWHAZ; NbExp=2; IntAct=EBI-618295, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15037601}.
Golgi apparatus {ECO:0000269|PubMed:15037601}. Note=Localizes to
the Golgi apparatus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O00506-1; Sequence=Displayed;
Name=2;
IsoId=O00506-2; Sequence=VSP_054397;
Note=No experimental confirmation available.;
Name=3;
IsoId=O00506-3; Sequence=VSP_054683;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels are
found in testis, large intestine, brain and stomach followed by
heart and lung.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/stk25/";
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EMBL; X99325; CAA67700.1; -; mRNA.
EMBL; D63780; BAA20420.1; -; mRNA.
EMBL; AK291808; BAF84497.1; -; mRNA.
EMBL; AK291947; BAF84636.1; -; mRNA.
EMBL; AK315966; BAH14337.1; -; mRNA.
EMBL; BT019961; AAV38764.1; -; mRNA.
EMBL; AC110299; AAY14683.1; -; Genomic_DNA.
EMBL; DQ093965; AAY88740.1; -; Genomic_DNA.
EMBL; CH471063; EAW71265.1; -; Genomic_DNA.
EMBL; BC007852; AAH07852.1; -; mRNA.
EMBL; BC091505; AAH91505.1; -; mRNA.
CCDS; CCDS2549.1; -. [O00506-1]
CCDS; CCDS63199.1; -. [O00506-3]
CCDS; CCDS63200.1; -. [O00506-2]
PIR; S71886; S71886.
RefSeq; NP_001258906.1; NM_001271977.1. [O00506-1]
RefSeq; NP_001258907.1; NM_001271978.1. [O00506-1]
RefSeq; NP_001258908.1; NM_001271979.1. [O00506-2]
RefSeq; NP_001258909.1; NM_001271980.1. [O00506-2]
RefSeq; NP_001269234.1; NM_001282305.1. [O00506-3]
RefSeq; NP_001269236.1; NM_001282307.1. [O00506-3]
RefSeq; NP_001269237.1; NM_001282308.1. [O00506-3]
RefSeq; NP_006365.2; NM_006374.4. [O00506-1]
UniGene; Hs.516807; -.
PDB; 2XIK; X-ray; 1.97 A; A=1-293.
PDB; 3W8H; X-ray; 2.43 A; B=355-426.
PDB; 4NZW; X-ray; 3.58 A; B=1-293.
PDBsum; 2XIK; -.
PDBsum; 3W8H; -.
PDBsum; 4NZW; -.
ProteinModelPortal; O00506; -.
SMR; O00506; -.
BioGrid; 115757; 53.
DIP; DIP-34269N; -.
IntAct; O00506; 43.
MINT; MINT-2997826; -.
STRING; 9606.ENSP00000325748; -.
BindingDB; O00506; -.
ChEMBL; CHEMBL5552; -.
GuidetoPHARMACOLOGY; 2218; -.
iPTMnet; O00506; -.
PhosphoSitePlus; O00506; -.
SwissPalm; O00506; -.
EPD; O00506; -.
MaxQB; O00506; -.
PaxDb; O00506; -.
PeptideAtlas; O00506; -.
PRIDE; O00506; -.
DNASU; 10494; -.
Ensembl; ENST00000316586; ENSP00000325748; ENSG00000115694. [O00506-1]
Ensembl; ENST00000401869; ENSP00000385687; ENSG00000115694. [O00506-1]
Ensembl; ENST00000403346; ENSP00000384162; ENSG00000115694. [O00506-1]
Ensembl; ENST00000405585; ENSP00000385541; ENSG00000115694. [O00506-2]
Ensembl; ENST00000405883; ENSP00000384444; ENSG00000115694. [O00506-2]
Ensembl; ENST00000535007; ENSP00000446008; ENSG00000115694. [O00506-3]
Ensembl; ENST00000543554; ENSP00000444886; ENSG00000115694. [O00506-3]
GeneID; 10494; -.
KEGG; hsa:10494; -.
UCSC; uc002wbm.5; human. [O00506-1]
CTD; 10494; -.
DisGeNET; 10494; -.
EuPathDB; HostDB:ENSG00000115694.14; -.
GeneCards; STK25; -.
HGNC; HGNC:11404; STK25.
HPA; HPA047147; -.
MIM; 602255; gene.
neXtProt; NX_O00506; -.
OpenTargets; ENSG00000115694; -.
PharmGKB; PA36211; -.
eggNOG; KOG0201; Eukaryota.
eggNOG; ENOG410XP9G; LUCA.
GeneTree; ENSGT00810000125395; -.
HOGENOM; HOG000234203; -.
HOVERGEN; HBG108518; -.
InParanoid; O00506; -.
KO; K08838; -.
OMA; FSHNRNH; -.
OrthoDB; EOG091G0F24; -.
PhylomeDB; O00506; -.
TreeFam; TF354217; -.
SignaLink; O00506; -.
SIGNOR; O00506; -.
ChiTaRS; STK25; human.
GeneWiki; STK25; -.
GenomeRNAi; 10494; -.
PRO; PR:O00506; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115694; -.
CleanEx; HS_STK25; -.
ExpressionAtlas; O00506; baseline and differential.
Genevisible; O00506; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
GO; GO:0051645; P:Golgi localization; IDA:UniProtKB.
GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB.
GO; GO:0036481; P:intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IGI:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd06642; STKc_STK25; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR035060; STK_STK25.
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; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Golgi apparatus; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 426 Serine/threonine-protein kinase 25.
/FTId=PRO_0000086713.
DOMAIN 20 270 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 26 34 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 140 140 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 49 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 174 174 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:15037601}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2W1}.
VAR_SEQ 1 94 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054683.
VAR_SEQ 11 87 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054397.
VARIANT 64 64 Q -> H (in dbSNP:rs34341643).
/FTId=VAR_051674.
MUTAGEN 49 49 K->R: Loss of kinase activity and
autophosphorylation.
{ECO:0000269|PubMed:15037601}.
MUTAGEN 158 158 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:15037601}.
CONFLICT 347 348 EP -> DA (in Ref. 1; CAA67700).
{ECO:0000305}.
TURN 5 7 {ECO:0000244|PDB:2XIK}.
HELIX 8 10 {ECO:0000244|PDB:2XIK}.
HELIX 16 19 {ECO:0000244|PDB:2XIK}.
STRAND 20 28 {ECO:0000244|PDB:2XIK}.
STRAND 30 39 {ECO:0000244|PDB:2XIK}.
TURN 40 42 {ECO:0000244|PDB:2XIK}.
STRAND 45 52 {ECO:0000244|PDB:2XIK}.
TURN 53 56 {ECO:0000244|PDB:2XIK}.
HELIX 60 72 {ECO:0000244|PDB:2XIK}.
STRAND 81 87 {ECO:0000244|PDB:2XIK}.
STRAND 90 96 {ECO:0000244|PDB:2XIK}.
HELIX 103 107 {ECO:0000244|PDB:2XIK}.
HELIX 114 133 {ECO:0000244|PDB:2XIK}.
HELIX 143 145 {ECO:0000244|PDB:2XIK}.
STRAND 146 148 {ECO:0000244|PDB:2XIK}.
STRAND 154 156 {ECO:0000244|PDB:2XIK}.
STRAND 170 172 {ECO:0000244|PDB:2XIK}.
HELIX 179 181 {ECO:0000244|PDB:2XIK}.
HELIX 184 187 {ECO:0000244|PDB:2XIK}.
HELIX 195 210 {ECO:0000244|PDB:2XIK}.
TURN 214 217 {ECO:0000244|PDB:2XIK}.
HELIX 220 226 {ECO:0000244|PDB:2XIK}.
TURN 227 229 {ECO:0000244|PDB:2XIK}.
HELIX 241 250 {ECO:0000244|PDB:2XIK}.
HELIX 255 257 {ECO:0000244|PDB:2XIK}.
HELIX 261 264 {ECO:0000244|PDB:2XIK}.
HELIX 268 272 {ECO:0000244|PDB:2XIK}.
HELIX 277 280 {ECO:0000244|PDB:2XIK}.
HELIX 281 291 {ECO:0000244|PDB:2XIK}.
HELIX 357 360 {ECO:0000244|PDB:3W8H}.
HELIX 362 374 {ECO:0000244|PDB:3W8H}.
TURN 375 377 {ECO:0000244|PDB:3W8H}.
HELIX 381 396 {ECO:0000244|PDB:3W8H}.
HELIX 400 414 {ECO:0000244|PDB:3W8H}.
SEQUENCE 426 AA; 48112 MW; 183CE5700FCEA716 CRC64;
MAHLRGFANQ HSRVDPEELF TKLDRIGKGS FGEVYKGIDN HTKEVVAIKI IDLEEAEDEI
EDIQQEITVL SQCDSPYITR YFGSYLKSTK LWIIMEYLGG GSALDLLKPG PLEETYIATI
LREILKGLDY LHSERKIHRD IKAANVLLSE QGDVKLADFG VAGQLTDTQI KRNTFVGTPF
WMAPEVIKQS AYDFKADIWS LGITAIELAK GEPPNSDLHP MRVLFLIPKN SPPTLEGQHS
KPFKEFVEAC LNKDPRFRPT AKELLKHKFI TRYTKKTSFL TELIDRYKRW KSEGHGEESS
SEDSDIDGEA EDGEQGPIWT FPPTIRPSPH SKLHKGTALH SSQKPAEPVK RQPRSQCLST
LVRPVFGELK EKHKQSGGSV GALEELENAF SLAEESCPGI SDKLMVHLVE RVQRFSHNRN
HLTSTR


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Catalog number Product name Quantity
EIAAB40306 Homo sapiens,Human,Serine_threonine-protein kinase 25,SOK1,SOK-1,Ste20_oxidant stress response kinase 1,Ste20-like kinase,Sterile 20_oxidant stress-response kinase 1,STK25,YSK1
EIAAB40307 Mouse,Mus musculus,Serine_threonine-protein kinase 25,Sok1,SOK-1,Ste20_oxidant stress response kinase 1,Ste20-like kinase,Sterile 20_oxidant stress-response kinase 1,Stk25
26-096 MAP4K1 belongs to the protein kinase superfamily, STE Ser_Thr protein kinase family, STE20 subfamily. MAP4K1 may play a role in the response to environmental stress. It appears to act upstream of the 0.05 mg
30-444 STK39 is a serine_threonine kinase that is thought to function in the cellular stress response pathway. The kinase is activated in response to hypotonic stress, leading to phosphorylation of several c 0.05 mg
30-443 STK39 is a serine_threonine kinase that is thought to function in the cellular stress response pathway. The kinase is activated in response to hypotonic stress, leading to phosphorylation of several c 0.1 mg
EIAAB38677 Etk4,Kiaa0204,Mouse,mSLK,Mus musculus,Serine_threonine-protein kinase 2,Slk,STE20-like kinase,STE20-like serine_threonine-protein kinase,STE20-related kinase,STE20-related kinase SMAK,STE20-related se
EIAAB38676 CTCL tumor antigen se20-9,Homo sapiens,hSLK,Human,KIAA0204,Serine_threonine-protein kinase 2,SLK,STE20-like kinase,STE20-like serine_threonine-protein kinase,STE20-related kinase,STE20-related serine_
EIAAB38678 Rat,Rattus norvegicus,Sk2,Slk,STE20-like kinase,STE20-like serine_threonine-protein kinase,STE20-related kinase,STE20-related serine_threonine-protein kinase
EIAAB41366 hKFC-B,Homo sapiens,hTAOK1,Human,KIAA1361,Kinase from chicken homolog B,MAP3K16,MARK Kinase,MARKK,MARKK,Prostate-derived STE20-like kinase 2,Prostate-derived sterile 20-like kinase 2,PSK2,PSK-2,Serine
EIAAB40304 Homo sapiens,Human,Mammalian STE20-like protein kinase 3,MST3,MST-3,Serine_threonine-protein kinase 24,STE20-like kinase MST3,STK24,STK3
EIAAB40305 Mammalian STE20-like protein kinase 3,Mst3,MST-3,MST3b,Rat,Rattus norvegicus,Serine_threonine-protein kinase 24,STE20-like kinase MST3,Stk24,Stk3
EIAAB40303 Mammalian STE20-like protein kinase 3,Mouse,Mst3,MST-3,Mus musculus,Serine_threonine-protein kinase 24,STE20-like kinase MST3,Stk24,Stk3
EIAAB40311 Mammalian STE20-like protein kinase 2,Mess1,Mouse,Mst2,MST-2,Mus musculus,Serine_threonine-protein kinase 3,STE20-like kinase MST2,Stk3
EIAAB25549 Homo sapiens,Human,Mammalian STE20-like protein kinase 4,MASK,Mst3 and SOK1-related kinase,MST4,MST-4,Serine_threonine-protein kinase MASK,Serine_threonine-protein kinase MST4,STE20-like kinase MST4
EIAAB24855 c-Jun N-terminal kinase 1,Homo sapiens,Human,JNK1,JNK-46,MAP kinase 8,MAPK 8,MAPK8,Mitogen-activated protein kinase 8,PRKM8,SAPK1,Stress-activated protein kinase 1,Stress-activated protein kinase JNK1
EIAAB40329 Mammalian STE20-like protein kinase 1,Mouse,Mst1,MST-1,Mus musculus,Serine_threonine-protein kinase 4,STE20-like kinase MST1,Stk4
EIAAB40310 Mammalian STE20-like protein kinase 2,Mst2,MST-2,Rat,Rattus norvegicus,Serine_threonine-protein kinase 3,STE20-like kinase MST2,Stk3
EIAAB40328 Bos taurus,Bovine,Mammalian STE20-like protein kinase 1,MST1,MST-1,Serine_threonine-protein kinase 4,STE20-like kinase MST1,STK4
EIAAB40309 Homo sapiens,Human,Mammalian STE20-like protein kinase 2,MST2,MST-2,Serine_threonine-protein kinase 3,Serine_threonine-protein kinase Krs-1,STE20-like kinase MST2,STK3
EIAAB40330 Homo sapiens,Human,Mammalian STE20-like protein kinase 1,MST1,MST-1,Serine_threonine-protein kinase 4,Serine_threonine-protein kinase Krs-2,STE20-like kinase MST1,STK4
H3180 STE20-like serine threonine-protein kinase (SLK), Rat, ELISA Kit 96T
H3177 STE20-like serine threonine-protein kinase (SLK), Guinea pig, ELISA Kit 96T
H3178 STE20-like serine threonine-protein kinase (SLK), Human, ELISA Kit 96T
H3179 STE20-like serine threonine-protein kinase (SLK), Mouse, ELISA Kit 96T
SLK_RAT ELISA Kit FOR STE20-like serine per threonine-protein kinase; organism: Rat; gene name: Slk 96T


 

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