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Non-receptor tyrosine-protein kinase TNK1 (EC 2.7.10.2) (CD38 negative kinase 1)

 TNK1_HUMAN              Reviewed;         666 AA.
Q13470; O95364; Q8IYI4;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
07-NOV-2018, entry version 156.
RecName: Full=Non-receptor tyrosine-protein kinase TNK1;
EC=2.7.10.2;
AltName: Full=CD38 negative kinase 1;
Name=TNK1 {ECO:0000312|EMBL:AAC99412.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC50427.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-598, TISSUE
SPECIFICITY, AND CHROMOSOMAL LOCATION.
TISSUE=Umbilical cord blood {ECO:0000312|EMBL:AAC50427.1};
PubMed=8632913;
Hoehn G.T., Stokland T., Amin S., Ramirez M., Hawkins A.L.,
Griffin C.A., Small D., Civin C.I.;
"Tnk1: a novel intracellular tyrosine kinase gene isolated from human
umbilical cord blood CD34+/Lin-/CD38- stem/progenitor cells.";
Oncogene 12:903-913(1996).
[2] {ECO:0000312|EMBL:AAC99412.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-598.
Hoehn G.T., Felschow D.M., Civin C.I.;
"Genomic structure and chromosomal mapping of the human non-receptor
tyrosine kinase gene, Tnk1.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:AAH35782.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Ovary {ECO:0000312|EMBL:AAH35782.1};
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).
[4] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AUTOPHOSPHORYLATION, AND INTERACTION WITH PLCG1.
PubMed=10873601; DOI=10.1006/bbrc.2000.2887;
Felschow D.M., Civin C.I., Hoehn G.T.;
"Characterization of the tyrosine kinase Tnk1 and its binding with
phospholipase C-gamma1.";
Biochem. Biophys. Res. Commun. 273:294-301(2000).
[5]
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).
[6]
FUNCTION.
PubMed=18974114; DOI=10.1158/0008-5472.CAN-08-1467;
Hoare S., Hoare K., Reinhard M.K., Lee Y.J., Oh S.P., May W.S. Jr.;
"Tnk1/Kos1 knockout mice develop spontaneous tumors.";
Cancer Res. 68:8723-8732(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-255; SER-502;
THR-514 AND SER-582, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411
(ISOFORM 2), AND 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-519, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-502,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 (ISOFORM 2), AND
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND THR-514, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-502, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
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).
[14]
VARIANTS [LARGE SCALE ANALYSIS] ILE-278; LYS-339; LYS-514; CYS-539;
CYS-546 AND MET-598.
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: Involved in negative regulation of cell growth. Has
tumor suppressor properties. Plays a negative regulatory role in
the Ras-MAPK pathway. May function in signaling pathways utilized
broadly during fetal development and more selectively in adult
tissues and in cells of the lymphohematopoietic system. Could
specifically be involved in phospholipid signal transduction.
{ECO:0000269|PubMed:10873601, ECO:0000269|PubMed:18974114}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Interacts with the SH3 domain of PLCG1 via its Pro-rich
domain. {ECO:0000269|PubMed:10873601}.
-!- INTERACTION:
P31947:SFN; NbExp=2; IntAct=EBI-1383444, EBI-476295;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10873601}.
Membrane {ECO:0000269|PubMed:10873601}; Peripheral membrane
protein {ECO:0000269|PubMed:10873601}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:8632913};
IsoId=Q13470-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q13470-2; Sequence=VSP_051663;
Note=No experimental confirmation available. Contains a
phosphoserine at position 411. {ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195};
-!- TISSUE SPECIFICITY: Expressed in all umbilical cord blood, bone
marrow and adult blood cell sub-populations and in several
leukemia cell lines. Highly expressed in fetal blood, brain, lung,
liver and kidney. Detected at lower levels in adult prostate,
testis, ovary, small intestine and colon. Not expressed in adult
lung, liver, kidney or brain. {ECO:0000269|PubMed:10873601,
ECO:0000269|PubMed:8632913}.
-!- PTM: Autophosphorylated on tyrosine residues.
{ECO:0000269|PubMed:10873601}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; U43408; AAC50427.1; -; mRNA.
EMBL; AF097738; AAC99412.1; -; Genomic_DNA.
EMBL; BC035782; AAH35782.1; -; mRNA.
CCDS; CCDS45602.1; -. [Q13470-2]
CCDS; CCDS58510.1; -. [Q13470-1]
RefSeq; NP_001238831.1; NM_001251902.1. [Q13470-1]
RefSeq; NP_003976.2; NM_003985.4. [Q13470-2]
RefSeq; XP_011522347.1; XM_011524045.2. [Q13470-2]
UniGene; Hs.203420; -.
UniGene; Hs.739114; -.
ProteinModelPortal; Q13470; -.
SMR; Q13470; -.
BioGrid; 114253; 25.
IntAct; Q13470; 32.
MINT; Q13470; -.
STRING; 9606.ENSP00000312309; -.
BindingDB; Q13470; -.
ChEMBL; CHEMBL5334; -.
GuidetoPHARMACOLOGY; 2245; -.
GlyConnect; 1575; -.
iPTMnet; Q13470; -.
PhosphoSitePlus; Q13470; -.
BioMuta; TNK1; -.
DMDM; 116242821; -.
MaxQB; Q13470; -.
PaxDb; Q13470; -.
PeptideAtlas; Q13470; -.
PRIDE; Q13470; -.
ProteomicsDB; 59467; -.
ProteomicsDB; 59468; -. [Q13470-2]
DNASU; 8711; -.
Ensembl; ENST00000570896; ENSP00000458834; ENSG00000174292. [Q13470-2]
Ensembl; ENST00000576812; ENSP00000459799; ENSG00000174292. [Q13470-1]
Ensembl; ENST00000639010; ENSP00000491712; ENSG00000283781. [Q13470-2]
Ensembl; ENST00000639430; ENSP00000491136; ENSG00000283781. [Q13470-1]
GeneID; 8711; -.
KEGG; hsa:8711; -.
UCSC; uc002ggi.5; human. [Q13470-1]
CTD; 8711; -.
DisGeNET; 8711; -.
EuPathDB; HostDB:ENSG00000174292.12; -.
GeneCards; TNK1; -.
HGNC; HGNC:11940; TNK1.
HPA; HPA012065; -.
HPA; HPA056452; -.
MIM; 608076; gene.
neXtProt; NX_Q13470; -.
OpenTargets; ENSG00000174292; -.
PharmGKB; PA36630; -.
eggNOG; KOG0199; Eukaryota.
eggNOG; ENOG410XPRC; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000231055; -.
HOVERGEN; HBG055513; -.
InParanoid; Q13470; -.
KO; K08885; -.
OMA; DPITVIE; -.
OrthoDB; EOG091G03HT; -.
PhylomeDB; Q13470; -.
TreeFam; TF316643; -.
ChiTaRS; TNK1; human.
GenomeRNAi; 8711; -.
PRO; PR:Q13470; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000174292; Expressed in 156 organ(s), highest expression level in nasal cavity epithelium.
CleanEx; HS_TNK1; -.
ExpressionAtlas; Q13470; baseline and differential.
Genevisible; Q13470; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; SH3 domain; Transferase; Tyrosine-protein kinase.
CHAIN 1 666 Non-receptor tyrosine-protein kinase
TNK1.
/FTId=PRO_0000088173.
DOMAIN 116 377 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 380 445 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
NP_BIND 122 130 ATP. {ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159}.
COMPBIAS 511 573 Pro-rich.
ACT_SITE 245 245 Proton acceptor.
{ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028}.
BINDING 148 148 ATP. {ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 514 514 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 411 415 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051663.
VARIANT 278 278 V -> I (in dbSNP:rs55939858).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041863.
VARIANT 339 339 R -> K (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041864.
VARIANT 514 514 T -> K (in dbSNP:rs55641092).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041865.
VARIANT 539 539 R -> C (in dbSNP:rs36046975).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041866.
VARIANT 546 546 S -> C (in dbSNP:rs56093628).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041867.
VARIANT 598 598 V -> M (in dbSNP:rs6503018).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8632913,
ECO:0000269|Ref.2}.
/FTId=VAR_041868.
CONFLICT 36 36 E -> G (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 65 65 R -> S (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 94 94 S -> T (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 118 118 R -> K (in Ref. 2; AAC99412).
{ECO:0000305}.
CONFLICT 252 252 L -> Q (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 288 288 A -> T (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 325 325 A -> P (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 347 348 LC -> PS (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 391 391 V -> A (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 424 424 G -> D (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 443 443 A -> T (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 561 561 K -> E (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 604 604 G -> W (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 622 622 V -> A (in Ref. 1; AAC50427).
{ECO:0000305}.
CONFLICT 635 635 H -> L (in Ref. 1; AAC50427).
{ECO:0000305}.
SEQUENCE 666 AA; 72468 MW; AA7FBEF6CC778181 CRC64;
MLPEAGSLWL LKLLRDIQLA QFYWPILEEL NVTRPEHFDF VKPEDLDGIG MGRPAQRRLS
EALKRLRSGP KSKNWVYKIL GGFAPEHKEP TLPSDSPRHL PEPEGGLKCL IPEGAVCRGE
LLGSGCFGVV HRGLWTLPSG KSVPVAVKSL RVGPEGPMGT ELGDFLREVS VMMNLEHPHV
LRLHGLVLGQ PLQMVMELAP LGSLHARLTA PAPTPPLLVA LLCLFLRQLA GAMAYLGARG
LVHRDLATRN LLLASPRTIK VADFGLVRPL GGARGRYVMG GPRPIPYAWC APESLRHGAF
SSASDVWMFG VTLWEMFSGG EEPWAGVPPY LILQRLEDRA RLPRPPLCSR ALYSLALRCW
APHPADRPSF SHLEGLLQEA GPSEACCVRD VTEPGALRME TGDPITVIEG SSSFHSPDST
IWKGQNGRTF KVGSFPASAV TLADAGGLPA TRPVHRGTPA RGDQHPGSID GDRKKANLWD
APPARGQRRN MPLERMKGIS RSLESVLSLG PRPTGGGSSP PEIRQARAVP QGPPGLPPRP
PLSSSSPQPS QPSRERLPWP KRKPPHNHPM GMPGARKAAA LSGGLLSDPE LQRKIMEVEL
SVHGVTHQEC QTALGATGGD VVSAIRNLKV DQLFHLSSRS RADCWRILEH YQWDLSAASR
YVLARP


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U0039m CLIA Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase receptor fl 96T
E0039m ELISA Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase receptor f 96T
E0039m ELISA kit Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase recep 96T
EIAAB13100 EK6,ELK,ELK,EPH tyrosine kinase 2,EPHB1,EPH-like kinase 6,Ephrin type-B receptor 1,EPHT2,hEK6,HEK6,Homo sapiens,Human,NET,NET,Neuronally-expressed EPH-related tyrosine kinase,Tyrosine-protein kinase r
EIAAB42378 Angiopoietin-1 receptor,Homo sapiens,hTIE2,Human,p140 TEK,TEK,TIE2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB42377 Angiopoietin-1 receptor,HYK,Hyk,Mouse,mTIE2,Mus musculus,p140 TEK,STK1,Tek,Tie2,Tie-2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
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
GWB-4F8FE2 Anti- Non-receptor tyrosine-protein kinase TNK1 Antibody


 

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