Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Serine/threonine-protein kinase ICK (EC 2.7.11.1) (Intestinal cell kinase) (hICK) (Laryngeal cancer kinase 2) (LCK2) (MAK-related kinase) (MRK)

 ICK_HUMAN               Reviewed;         632 AA.
Q9UPZ9; A7MD41; O75985; Q5THL2; Q8IYH8; Q9BX17; Q9NYX3;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 159.
RecName: Full=Serine/threonine-protein kinase ICK;
EC=2.7.11.1 {ECO:0000269|PubMed:10699974};
AltName: Full=Intestinal cell kinase;
Short=hICK;
AltName: Full=Laryngeal cancer kinase 2;
Short=LCK2;
AltName: Full=MAK-related kinase;
Short=MRK;
Name=ICK; Synonyms=KIAA0936;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF37278.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF
LYS-33; LYS-34; LYS-36; LYS-38; THR-157 AND TYR-159, AND
PHOSPHORYLATION AT THR-157 AND TYR-159.
TISSUE=Colon {ECO:0000269|PubMed:10699974};
PubMed=10699974;
DOI=10.1002/(SICI)1097-4652(200004)183:1<129::AID-JCP15>3.0.CO;2-S;
Togawa K., Yan Y.-X., Inomoto T., Slaugenhaupt S.A., Rustgi A.K.;
"Intestinal cell kinase (ICK) localizes to the crypt region and
requires a dual phosphorylation site found in map kinases.";
J. Cell. Physiol. 183:129-139(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=12103360; DOI=10.1016/S1389-0344(02)00002-3;
Yang T., Jiang Y., Chen J.;
"The identification and subcellular localization of human MRK.";
Biomol. Eng. 19:1-4(2002).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain {ECO:0000312|EMBL:BAA76780.2};
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5] {ECO:0000305}
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.
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain {ECO:0000312|EMBL:AAH35807.1};
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT ECO
GLN-272.
PubMed=24797473; DOI=10.1002/embj.201488175;
Chaya T., Omori Y., Kuwahara R., Furukawa T.;
"ICK is essential for cell type-specific ciliogenesis and the
regulation of ciliary transport.";
EMBO J. 33:1227-1242(2014).
[10]
FUNCTION, AND CHARACTERIZATION OF VARIANT ECO GLN-272.
PubMed=24853502; DOI=10.1073/pnas.1323161111;
Moon H., Song J., Shin J.O., Lee H., Kim H.K., Eggenschwiller J.T.,
Bok J., Ko H.W.;
"Intestinal cell kinase, a protein associated with endocrine-cerebro-
osteodysplasia syndrome, is a key regulator of cilia length and
Hedgehog signaling.";
Proc. Natl. Acad. Sci. U.S.A. 111:8541-8546(2014).
[11]
VARIANTS [LARGE SCALE ANALYSIS] TYR-115; ILE-320; LYS-471; GLN-476 AND
THR-615.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[12]
VARIANT ECO GLN-272, CHARACTERIZATION OF VARIANT ECO GLN-272, AND
POSSIBLE FUNCTION.
PubMed=19185282; DOI=10.1016/j.ajhg.2008.12.017;
Lahiry P., Wang J., Robinson J.F., Turowec J.P., Litchfield D.W.,
Lanktree M.B., Gloor G.B., Puffenberger E.G., Strauss K.A.,
Martens M.B., Ramsay D.A., Rupar C.A., Siu V., Hegele R.A.;
"A multiplex human syndrome implicates a key role for intestinal cell
kinase in development of central nervous, skeletal, and endocrine
systems.";
Am. J. Hum. Genet. 84:134-147(2009).
-!- FUNCTION: Required for ciliogenesis (PubMed:24797473).
Phosphorylates KIF3A (By similarity). Involved in the control of
ciliary length (PubMed:24853502). Regulates the ciliary
localization of SHH pathway components as well as the localization
of IFT components at ciliary tips (By similarity). May play a key
role in the development of multiple organ systems and particularly
in cardiac development (By similarity). Regulates intraflagellar
transport (IFT) speed and negatively regulates cilium length in a
cAMP and mTORC1 signaling-dependent manner and this regulation
requires its kinase activity (By similarity).
{ECO:0000250|UniProtKB:Q62726, ECO:0000250|UniProtKB:Q9JKV2,
ECO:0000269|PubMed:24797473, ECO:0000269|PubMed:24853502}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10699974}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10699974};
-!- INTERACTION:
P08238:HSP90AB1; NbExp=2; IntAct=EBI-6381479, EBI-352572;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12103360}.
Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q62726}. Cell
projection, cilium {ECO:0000269|PubMed:24797473}. Cytoplasm,
cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9JKV2}.
Note=Also found at the ciliary tip (PubMed:24797473). Nuclear
localization has been observed with a GFP-tagged construct in
transfected HeLa cells (PubMed:12103360).
{ECO:0000269|PubMed:12103360, ECO:0000269|PubMed:24797473}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:10699974};
IsoId=Q9UPZ9-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q9UPZ9-2; Sequence=VSP_050752, VSP_050753;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, pancreas,
thymus, prostate, testis, ovary, small intestine and colon, with
highest levels in placenta and testis. Not detected in spleen.
Also expressed in many cancer cell lines.
{ECO:0000269|PubMed:10699974, ECO:0000269|PubMed:12103360}.
-!- PTM: Autophosphorylated on serine and threonine residues. May play
a role in enzyme activation. {ECO:0000269|PubMed:10699974}.
-!- DISEASE: Endocrine-cerebroosteodysplasia (ECO) [MIM:612651]:
Previously unidentified neonatal lethal recessive disorder with
multiple anomalies involving the endocrine, cerebral, and skeletal
systems. {ECO:0000269|PubMed:19185282,
ECO:0000269|PubMed:24797473, ECO:0000269|PubMed:24853502}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA76780.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF225919; AAF37278.1; -; mRNA.
EMBL; AF152469; AAG43364.1; -; mRNA.
EMBL; AB023153; BAA76780.2; ALT_INIT; mRNA.
EMBL; AL031178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL162581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX04400.1; -; Genomic_DNA.
EMBL; BC035807; AAH35807.1; -; mRNA.
EMBL; BC136420; AAI36421.1; -; mRNA.
EMBL; BC136421; AAI36422.1; -; mRNA.
EMBL; BC152464; AAI52465.1; -; mRNA.
CCDS; CCDS4949.1; -. [Q9UPZ9-1]
RefSeq; NP_055735.1; NM_014920.3. [Q9UPZ9-1]
RefSeq; NP_057597.2; NM_016513.4. [Q9UPZ9-1]
RefSeq; XP_016865977.1; XM_017010488.1. [Q9UPZ9-1]
RefSeq; XP_016865978.1; XM_017010489.1. [Q9UPZ9-1]
RefSeq; XP_016865979.1; XM_017010490.1. [Q9UPZ9-1]
RefSeq; XP_016865980.1; XM_017010491.1. [Q9UPZ9-1]
RefSeq; XP_016865981.1; XM_017010492.1. [Q9UPZ9-1]
UniGene; Hs.417022; -.
ProteinModelPortal; Q9UPZ9; -.
SMR; Q9UPZ9; -.
BioGrid; 116527; 40.
IntAct; Q9UPZ9; 10.
MINT; Q9UPZ9; -.
STRING; 9606.ENSP00000263043; -.
BindingDB; Q9UPZ9; -.
ChEMBL; CHEMBL1163126; -.
GuidetoPHARMACOLOGY; 2038; -.
iPTMnet; Q9UPZ9; -.
PhosphoSitePlus; Q9UPZ9; -.
BioMuta; ICK; -.
DMDM; 48428273; -.
EPD; Q9UPZ9; -.
PaxDb; Q9UPZ9; -.
PeptideAtlas; Q9UPZ9; -.
PRIDE; Q9UPZ9; -.
ProteomicsDB; 85480; -.
ProteomicsDB; 85481; -. [Q9UPZ9-2]
DNASU; 22858; -.
Ensembl; ENST00000350082; ENSP00000263043; ENSG00000112144. [Q9UPZ9-1]
Ensembl; ENST00000356971; ENSP00000349458; ENSG00000112144. [Q9UPZ9-1]
GeneID; 22858; -.
KEGG; hsa:22858; -.
UCSC; uc003pbh.3; human. [Q9UPZ9-1]
CTD; 22858; -.
DisGeNET; 22858; -.
EuPathDB; HostDB:ENSG00000112144.15; -.
GeneCards; ICK; -.
HGNC; HGNC:21219; ICK.
HPA; HPA000791; -.
HPA; HPA001113; -.
MalaCards; ICK; -.
MIM; 612325; gene.
MIM; 612651; phenotype.
neXtProt; NX_Q9UPZ9; -.
OpenTargets; ENSG00000112144; -.
Orphanet; 199332; Endocrine-cerebro-osteodysplasia syndrome.
PharmGKB; PA134894544; -.
eggNOG; KOG0661; Eukaryota.
eggNOG; ENOG410XPBB; LUCA.
GeneTree; ENSGT00650000093283; -.
HOVERGEN; HBG014652; -.
InParanoid; Q9UPZ9; -.
KO; K08828; -.
OMA; FHTQPRS; -.
OrthoDB; EOG091G0DU3; -.
PhylomeDB; Q9UPZ9; -.
TreeFam; TF328769; -.
SignaLink; Q9UPZ9; -.
SIGNOR; Q9UPZ9; -.
ChiTaRS; ICK; human.
GeneWiki; ICK_(gene); -.
GenomeRNAi; 22858; -.
PRO; PR:Q9UPZ9; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112144; -.
CleanEx; HS_ICK; -.
ExpressionAtlas; Q9UPZ9; baseline and differential.
Genevisible; Q9UPZ9; HS.
GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
GO; GO:0097542; C:ciliary tip; IMP:UniProtKB.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0035720; P:intraciliary anterograde transport; ISS:UniProtKB.
GO; GO:0035721; P:intraciliary retrograde transport; ISS:UniProtKB.
GO; GO:0042073; P:intraciliary transport; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell projection;
Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Disease mutation; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 632 Serine/threonine-protein kinase ICK.
/FTId=PRO_0000086007.
DOMAIN 4 284 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000305}.
NP_BIND 10 18 ATP. {ECO:0000250|UniProtKB:P06493,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 125 125 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:10699974}.
MOD_RES 157 157 Phosphothreonine.
{ECO:0000269|PubMed:10699974}.
MOD_RES 159 159 Phosphotyrosine.
{ECO:0000269|PubMed:10699974}.
VAR_SEQ 278 292 ALRYPYFQVGHPLGS -> VFFHFLVITFISNSE (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050752.
VAR_SEQ 293 632 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050753.
VARIANT 98 98 P -> L (in dbSNP:rs1493105).
/FTId=VAR_053931.
VARIANT 115 115 F -> Y (in a renal clear cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042001.
VARIANT 272 272 R -> Q (in ECO; significantly impairs
kinase activity; decreased localization
at the ciliary tips; impaired
ciliogenesis; results in abnormally
elongated cilia; dbSNP:rs118203918).
{ECO:0000269|PubMed:19185282,
ECO:0000269|PubMed:24797473,
ECO:0000269|PubMed:24853502}.
/FTId=VAR_057994.
VARIANT 320 320 V -> I (in dbSNP:rs33936662).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042002.
VARIANT 471 471 T -> K (in dbSNP:rs56164633).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042003.
VARIANT 476 476 R -> Q (in dbSNP:rs55895113).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042004.
VARIANT 615 615 A -> T (in dbSNP:rs55932059).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042005.
MUTAGEN 33 33 K->R: Loss of activity and
autophosphorylation; when associated with
R-34; R-36 and R-38.
{ECO:0000269|PubMed:10699974}.
MUTAGEN 34 34 K->R: Loss of activity and
autophosphorylation; when associated with
R-33; R-36 and R-38.
{ECO:0000269|PubMed:10699974}.
MUTAGEN 36 36 K->R: Loss of activity and
autophosphorylation; when associated with
R-33; R-34 and R-38.
{ECO:0000269|PubMed:10699974}.
MUTAGEN 38 38 K->R: Loss of activity and
autophosphorylation; when associated with
R-33; R-34 and R-36.
{ECO:0000269|PubMed:10699974}.
MUTAGEN 157 157 T->A: Reduction of activity and loss of
autophosphorylation. Loss of activity and
autophosphorylation; when associated with
F-159. {ECO:0000269|PubMed:10699974}.
MUTAGEN 159 159 Y->F: Reduction of activity and loss of
autophosphorylation. Loss of activity and
autophosphorylation; when associated with
A-157. {ECO:0000269|PubMed:10699974}.
CONFLICT 48 48 L -> Q (in Ref. 1; AAF37278).
{ECO:0000305}.
CONFLICT 119 119 H -> L (in Ref. 1; AAF37278).
{ECO:0000305}.
CONFLICT 310 310 K -> R (in Ref. 1; AAF37278).
{ECO:0000305}.
CONFLICT 598 599 FH -> LD (in Ref. 1; AAF37278).
{ECO:0000305}.
CONFLICT 629 629 A -> P (in Ref. 1; AAF37278).
{ECO:0000305}.
SEQUENCE 632 AA; 71427 MW; F4C22C6CCD5878D2 CRC64;
MNRYTTIRQL GDGTYGSVLL GRSIESGELI AIKKMKRKFY SWEECMNLRE VKSLKKLNHA
NVVKLKEVIR ENDHLYFIFE YMKENLYQLI KERNKLFPES AIRNIMYQIL QGLAFIHKHG
FFHRDLKPEN LLCMGPELVK IADFGLAREI RSKPPYTDYV STRWYRAPEV LLRSTNYSSP
IDVWAVGCIM AEVYTLRPLF PGASEIDTIF KICQVLGTPK KTDWPEGYQL SSAMNFRWPQ
CVPNNLKTLI PNASSEAVQL LRDMLQWDPK KRPTASQALR YPYFQVGHPL GSTTQNLQDS
EKPQKGILEK AGPPPYIKPV PPAQPPAKPH TRISSRQHQA SQPPLHLTYP YKAEVSRTDH
PSHLQEDKPS PLLFPSLHNK HPQSKITAGL EHKNGEIKPK SRRRWGLISR STKDSDDWAD
LDDLDFSPSL SRIDLKNKKR QSDDTLCRFE SVLDLKPSEP VGTGNSAPTQ TSYQRRDTPT
LRSAAKQHYL KHSRYLPGIS IRNGILSNPG KEFIPPNPWS SSGLSGKSSG TMSVISKVNS
VGSSSTSSSG LTGNYVPSFL KKEIGSAMQR VHLAPIPDPS PGYSSLKAMR PHPGRPFFHT
QPRSTPGLIP RPPAAQPVHG RTDWASKYAS RR


Related products :

Catalog number Product name Quantity
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
EIAAB24782 B55,GCK family kinase MiNK,Homo sapiens,Human,MAP4K6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,MINK,MINK1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated prote
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB31331 PAK-1,Pkn,Pkn1,Prk1,Prkcl1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Rat,Rattus norvegicus,Serine_threonine-protein kinase N1,Seri
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB06524 CAK-kinase p42,CCRK,CDCH,CDK20,CDK-activating kinase p42,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protein kinase H,Cyclin-kinase-activating
E1358m ELISA kit Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
U1358m CLIA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
EIAAB06503 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,CDK12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,CRK7,CrkRS,CRKRS,Cyclin-dependent kinase 12
EIAAB06502 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,Cdk12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,Crk7,CrkRS,Crkrs,Cyclin-dependent kinase 12
EIAAB06501 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,Cdk12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,Crk7,CrkRS,Crkrs,Cyclin-dependent kinase 12
E1358h ELISA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
U1358h CLIA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur