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N-terminal kinase-like protein (Coated vesicle-associated kinase of 90 kDa) (SCY1-like protein 1) (Telomerase regulation-associated protein) (Telomerase transcriptional element-interacting factor) (Teratoma-associated tyrosine kinase)

 SCYL1_HUMAN             Reviewed;         808 AA.
Q96KG9; A6NJF1; Q96G50; Q96KG8; Q96KH1; Q9HAW5; Q9HBL3; Q9NR53;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 146.
RecName: Full=N-terminal kinase-like protein;
AltName: Full=Coated vesicle-associated kinase of 90 kDa;
AltName: Full=SCY1-like protein 1;
AltName: Full=Telomerase regulation-associated protein;
AltName: Full=Telomerase transcriptional element-interacting factor;
AltName: Full=Teratoma-associated tyrosine kinase;
Name=SCYL1; Synonyms=CVAK90, GKLP, NTKL, TAPK, TEIF, TRAP;
ORFNames=HT019;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, AND TISSUE
SPECIFICITY.
TISSUE=Testis;
PubMed=12036289; DOI=10.1006/geno.2002.6774;
Kato M., Yano K., Morotomi-Yano K., Saito H., Miki Y.;
"Identification and characterization of the human protein kinase-like
gene NTKL: mitosis-specific centrosomal localization of an
alternatively spliced isoform.";
Genomics 79:760-767(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), DNA-BINDING (ISOFORM 6), AND
SUBCELLULAR LOCATION (ISOFORM 6).
TISSUE=Cervix carcinoma;
PubMed=15504359; DOI=10.1016/j.bbrc.2004.09.201;
Tang Z., Zhao Y., Mei F., Yang S., Li X., Lv J., Hou L., Zhang B.;
"Molecular cloning and characterization of a human gene involved in
transcriptional regulation of hTERT.";
Biochem. Biophys. Res. Commun. 324:1324-1332(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 310-808 (ISOFORM 4).
TISSUE=Eye, and Teratocarcinoma;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-283.
PubMed=10843802; DOI=10.1006/geno.2000.6194;
van Asseldonk M., Schepens M., de Bruijn D., Janssen B., Merkx G.,
Geurts van Kessel A.;
"Construction of a 350-kb sequence-ready 11q13 cosmid contig
encompassing the markers D11S4933 and D11S546: mapping of 11 genes and
3 tumor-associated translocation breakpoints.";
Genomics 66:35-42(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-808 (ISOFORM 5).
TISSUE=Hypothalamus;
Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION (ISOFORM 6), AND DNA-BINDING (ISOFORM 6).
PubMed=15963946; DOI=10.1016/j.bbrc.2005.05.172;
Zhao Y., Zheng J., Ling Y., Hou L., Zhang B.;
"Transcriptional upregulation of DNA polymerase beta by TEIF.";
Biochem. Biophys. Res. Commun. 333:908-916(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
INTERACTION WITH AP2B1.
PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
Mills I.G., Benmerah A., McMahon H.T.;
"Role of the AP2 beta-appendage hub in recruiting partners for
clathrin-coated vesicle assembly.";
PLoS Biol. 4:E262-E262(2006).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18556652; DOI=10.1074/jbc.M801869200;
Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y.,
Presley J.F., McPherson P.S.;
"Scyl1, mutated in a recessive form of spinocerebellar
neurodegeneration, regulates COPI-mediated retrograde traffic.";
J. Biol. Chem. 283:22774-22786(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
INVOLVEMENT IN SCAR21, AND FUNCTION.
PubMed=26581903; DOI=10.1016/j.ajhg.2015.10.011;
Schmidt W.M., Rutledge S.L., Schuele R., Mayerhofer B., Zuechner S.,
Boltshauser E., Bittner R.E.;
"Disruptive SCYL1 mutations underlie a syndrome characterized by
recurrent episodes of liver failure, peripheral neuropathy, cerebellar
atrophy, and ataxia.";
Am. J. Hum. Genet. 97:855-861(2015).
[16]
VARIANTS [LARGE SCALE ANALYSIS] LEU-479; TYR-495; HIS-663 AND SER-755.
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).
-!- FUNCTION: Regulates COPI-mediated retrograde protein traffic at
the interface between the Golgi apparatus and the endoplasmic
reticulum (PubMed:18556652). Involved in the maintenance of the
Golgi apparatus morphology (PubMed:26581903). Has no detectable
kinase activity in vitro (PubMed:18556652).
{ECO:0000269|PubMed:18556652, ECO:0000269|PubMed:26581903}.
-!- FUNCTION: Isoform 6 acts as transcriptional activator. It binds to
three different types of GC-rich DNA binding sites (box-A, -B and
-C) in the beta-polymerase promoter region. It also binds to the
TERT promoter region. {ECO:0000269|PubMed:18556652}.
-!- SUBUNIT: Interacts with GORAB. Interacts with COPA, COPB1 and
COPB2 (By similarity). Homooligomer. Interacts with AP2B1.
{ECO:0000250, ECO:0000269|PubMed:12036289,
ECO:0000269|PubMed:16903783}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:18556652}.
Endoplasmic reticulum-Golgi intermediate compartment
{ECO:0000269|PubMed:18556652}. Golgi apparatus, cis-Golgi network
{ECO:0000269|PubMed:18556652}. Note=Localized to the Endoplasmic
reticulum-Golgi intermediate and cis-Golgi in an ARF1-independent
manner.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Cytoplasmic
throughout the cell cycle.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Cytoplasmic
throughout the cell cycle.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Note=Cytoplasmic during interphase and centrosomal during mitosis,
it localizes to the centrosomes in a microtubule-independent
manner.
-!- SUBCELLULAR LOCATION: Isoform 6: Nucleus
{ECO:0000269|PubMed:15504359}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q96KG9-1; Sequence=Displayed;
Name=2; Synonyms=Variant 1;
IsoId=Q96KG9-2; Sequence=VSP_020504;
Name=3; Synonyms=Variant 2;
IsoId=Q96KG9-3; Sequence=VSP_020504, VSP_020506;
Note=Non-canonical splice junctions.;
Name=4;
IsoId=Q96KG9-4; Sequence=VSP_020508;
Name=5;
IsoId=Q96KG9-5; Sequence=VSP_020503, VSP_020505;
Name=6;
IsoId=Q96KG9-6; Sequence=VSP_020507;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12036289}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive.
-!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 21 (SCAR21)
[MIM:616719]: A form of spinocerebellar ataxia, a clinically and
genetically heterogeneous group of cerebellar disorders due to
degeneration of the cerebellum with variable involvement of the
brainstem and spinal cord. SCAR21 is characterized by cerebellar
atrophy and ataxia with onset in early childhood. Patients also
manifest recurrent episodes of liver failure, hepatic fibrosis and
a peripheral neuropathy. {ECO:0000269|PubMed:26581903}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG09726.1; Type=Frameshift; Positions=289, 307; Evidence={ECO:0000305};
Sequence=AAG17902.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AB047077; BAB55454.1; -; mRNA.
EMBL; AB051427; BAB55458.1; -; mRNA.
EMBL; AB051428; BAB55459.1; -; mRNA.
EMBL; AF297709; AAG17902.1; ALT_FRAME; mRNA.
EMBL; AP000769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74399.1; -; Genomic_DNA.
EMBL; BC009967; AAH09967.2; -; mRNA.
EMBL; BC069233; AAH69233.1; -; mRNA.
EMBL; AF255613; AAF81422.1; -; Genomic_DNA.
EMBL; AF225424; AAG09726.1; ALT_FRAME; mRNA.
CCDS; CCDS41672.1; -. [Q96KG9-1]
CCDS; CCDS44646.1; -. [Q96KG9-2]
RefSeq; NP_001041683.1; NM_001048218.1. [Q96KG9-2]
RefSeq; NP_065731.3; NM_020680.3. [Q96KG9-1]
RefSeq; XP_005274177.1; XM_005274120.3. [Q96KG9-4]
UniGene; Hs.238839; -.
ProteinModelPortal; Q96KG9; -.
BioGrid; 121512; 32.
CORUM; Q96KG9; -.
IntAct; Q96KG9; 23.
MINT; MINT-3055065; -.
STRING; 9606.ENSP00000270176; -.
DrugBank; DB05036; Grn163l.
iPTMnet; Q96KG9; -.
PhosphoSitePlus; Q96KG9; -.
BioMuta; SCYL1; -.
DMDM; 74762671; -.
EPD; Q96KG9; -.
MaxQB; Q96KG9; -.
PaxDb; Q96KG9; -.
PeptideAtlas; Q96KG9; -.
PRIDE; Q96KG9; -.
DNASU; 57410; -.
Ensembl; ENST00000270176; ENSP00000270176; ENSG00000142186. [Q96KG9-1]
Ensembl; ENST00000420247; ENSP00000408192; ENSG00000142186. [Q96KG9-2]
Ensembl; ENST00000533862; ENSP00000437254; ENSG00000142186. [Q96KG9-6]
GeneID; 57410; -.
KEGG; hsa:57410; -.
UCSC; uc001oea.2; human. [Q96KG9-1]
CTD; 57410; -.
DisGeNET; 57410; -.
EuPathDB; HostDB:ENSG00000142186.16; -.
GeneCards; SCYL1; -.
HGNC; HGNC:14372; SCYL1.
HPA; HPA015015; -.
MIM; 607982; gene.
MIM; 616719; phenotype.
neXtProt; NX_Q96KG9; -.
OpenTargets; ENSG00000142186; -.
PharmGKB; PA31812; -.
eggNOG; KOG1243; Eukaryota.
eggNOG; ENOG410XQTG; LUCA.
GeneTree; ENSGT00890000139451; -.
HOVERGEN; HBG082065; -.
InParanoid; Q96KG9; -.
KO; K08876; -.
OMA; EHESNDT; -.
OrthoDB; EOG091G02FF; -.
PhylomeDB; Q96KG9; -.
TreeFam; TF313435; -.
SignaLink; Q96KG9; -.
ChiTaRS; SCYL1; human.
GeneWiki; SCYL1; -.
GenomeRNAi; 57410; -.
PRO; PR:Q96KG9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000142186; -.
CleanEx; HS_SCYL1; -.
ExpressionAtlas; Q96KG9; baseline and differential.
Genevisible; Q96KG9; HS.
GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:HGNC.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
Pfam; PF00069; Pkinase; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; DNA-binding; ER-Golgi transport;
Golgi apparatus; Mental retardation; Neurodegeneration; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Spinocerebellar ataxia; Transcription; Transcription regulation;
Transport.
CHAIN 1 808 N-terminal kinase-like protein.
/FTId=PRO_0000249541.
DOMAIN 14 314 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REPEAT 350 388 HEAT 1.
REPEAT 389 427 HEAT 2.
REPEAT 507 545 HEAT 3.
REGION 793 808 Interaction with COPB1. {ECO:0000250}.
COILED 761 797 {ECO:0000255}.
COMPBIAS 589 619 Pro-rich.
MOD_RES 754 754 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 603 626 TPEGVPAPAPTPVPATPTTSGHWE -> SRPARRPLGDAGG
GQGHSRGQQHC (in isoform 5).
{ECO:0000303|Ref.7}.
/FTId=VSP_020503.
VAR_SEQ 606 622 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:12036289}.
/FTId=VSP_020504.
VAR_SEQ 627 808 Missing (in isoform 5).
{ECO:0000303|Ref.7}.
/FTId=VSP_020505.
VAR_SEQ 628 711 Missing (in isoform 3).
{ECO:0000303|PubMed:12036289}.
/FTId=VSP_020506.
VAR_SEQ 678 808 VSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDG
TRLASEYNWGGPESSDKGDPFATLSARPSTQPRPDSWGEDN
WEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPM
KLGARKLD -> SPTGAAGKLRAPGNRAGRSQAPRSHLLTV
HGWPASITGVAQSPATRATPSLPCLHVPAPSRGQTLGVRTT
GRASRLTVDRSRLSWPGRSARSGGGRWRPNAPRGRWPRAP
(in isoform 6).
{ECO:0000303|PubMed:15504359}.
/FTId=VSP_020507.
VAR_SEQ 750 808 PRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKR
AERKVAKGPMKLGARKLD -> DRSRLSWPGRSARSGGGRW
RPNAPRGRWPRAP (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020508.
VARIANT 479 479 P -> L (in dbSNP:rs55977709).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041364.
VARIANT 495 495 H -> Y (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041365.
VARIANT 663 663 Q -> H (in dbSNP:rs56076708).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041366.
VARIANT 755 755 W -> S (in dbSNP:rs56077405).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041367.
CONFLICT 168 169 GN -> AT (in Ref. 2; AAG17902).
{ECO:0000305}.
CONFLICT 530 530 I -> F (in Ref. 7; AAG09726).
{ECO:0000305}.
CONFLICT 574 574 V -> W (in Ref. 7; AAG09726).
{ECO:0000305}.
SEQUENCE 808 AA; 89631 MW; E87A2957DDCCE937 CRC64;
MWFFARDPVR DFPFELIPEP PEGGLPGPWA LHRGRKKATG SPVSIFVYDV KPGAEEQTQV
AKAAFKRFKT LRHPNILAYI DGLETEKCLH VVTEAVTPLG IYLKARVEAG GLKELEISWG
LHQIVKALSF LVNDCSLIHN NVCMAAVFVD RAGEWKLGGL DYMYSAQGNG GGPPRKGIPE
LEQYDPPELA DSSGRVVREK WSADMWRLGC LIWEVFNGPL PRAAALRNPG KIPKTLVPHY
CELVGANPKV RPNPARFLQN CRAPGGFMSN RFVETNLFLE EIQIKEPAEK QKFFQELSKS
LDAFPEDFCR HKVLPQLLTA FEFGNAGAVV LTPLFKVGKF LSAEEYQQKI IPVVVKMFSS
TDRAMRIRLL QQMEQFIQYL DEPTVNTQIF PHVVHGFLDT NPAIREQTVK SMLLLAPKLN
EANLNVELMK HFARLQAKDE QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATRDPF
APSRVAGVLG FAATHNLYSM NDCAQKILPV LCGLTVDPEK SVRDQAFKAI RSFLSKLESV
SEDPTQLEEV EKDVHAASSP GMGGAAASWA GWAVTGVSSL TSKLIRSHPT TAPTETNIPQ
RPTPEGVPAP APTPVPATPT TSGHWETQEE DKDTAEDSST ADRWDDEDWG SLEQEAESVL
AQQDDWSTGG QVSRASQVSN SDHKSSKSPE SDWSSWEAEG SWEQGWQEPS SQEPPPDGTR
LASEYNWGGP ESSDKGDPFA TLSARPSTQP RPDSWGEDNW EGLETDSRQV KAELARKKRE
ERRREMEAKR AERKVAKGPM KLGARKLD


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E0558r ELISA kit p230,p240,p80 telomerase homolog,Rat,Rattus norvegicus,rTLP1,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,Tep1,Tlp1 96T
U0558h CLIA Homo sapiens,Human,p240,p80 telomerase homolog,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,TEP1,TLP1,TP1 96T
E0558h ELISA Homo sapiens,Human,p240,p80 telomerase homolog,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,TEP1,TLP1,TP1 96T
E0558h ELISA kit Homo sapiens,Human,p240,p80 telomerase homolog,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,TEP1,TLP1,TP1 96T
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
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,
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
EIAAB33010 Inactive tyrosine-protein kinase 7,Mouse,Mus musculus,Protein chuzhoi,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,Ptk7,Tyrosine-protein kinase-like 7
U0558m CLIA Mouse,Mus musculus,p240,p80 telomerase homolog,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,Tep1,Tp1 96T
E0558m ELISA kit Mouse,Mus musculus,p240,p80 telomerase homolog,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,Tep1,Tp1 96T
E0558m ELISA Mouse,Mus musculus,p240,p80 telomerase homolog,Telomerase protein 1,Telomerase protein component 1,Telomerase-associated protein 1,Tep1,Tp1 96T
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
EIAAB33009 Chicken,Gallus gallus,Inactive tyrosine-protein kinase 7,Kinase-like protein,KLG,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
E1915m ELISA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
U1915m CLIA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
U1915m CLIA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T


 

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