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Proto-oncogene tyrosine-protein kinase ROS (EC 2.7.10.1) (Proto-oncogene c-Ros) (Proto-oncogene c-Ros-1) (Receptor tyrosine kinase c-ros oncogene 1) (c-Ros receptor tyrosine kinase)

 ROS1_MOUSE              Reviewed;        2340 AA.
Q78DX7; Q60705;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
18-JUL-2018, entry version 130.
RecName: Full=Proto-oncogene tyrosine-protein kinase ROS;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-Ros;
AltName: Full=Proto-oncogene c-Ros-1;
AltName: Full=Receptor tyrosine kinase c-ros oncogene 1;
AltName: Full=c-Ros receptor tyrosine kinase;
Flags: Precursor;
Name=Ros1; Synonyms=Ros, Ros-1;
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].
STRAIN=NMRI; TISSUE=Intestine;
PubMed=7970722;
Riethmacher D., Langholz O., Godecke S., Sachs M., Birchmeier C.;
"Biochemical and functional characterization of the murine ros
protooncogene.";
Oncogene 9:3617-3626(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD-1; TISSUE=Kidney;
PubMed=8544427; DOI=10.1038/ki.1995.460;
Kanwar Y.S., Liu Z.Z., Kumar A., Wada J., Carone F.A.;
"Cloning of mouse c-ros renal cDNA, its role in development and
relationship to extracellular matrix glycoproteins.";
Kidney Int. 48:1646-1659(1995).
[3]
DISRUPTION PHENOTYPE, FUNCTION IN EPITHELIUM DIFFERENTIATION, AND
TISSUE SPECIFICITY.
PubMed=8675006; DOI=10.1101/gad.10.10.1184;
Sonnenberg-Riethmacher E., Walter B., Riethmacher D., Goedecke S.,
Birchmeier C.;
"The c-ros tyrosine kinase receptor controls regionalization and
differentiation of epithelial cells in the epididymis.";
Genes Dev. 10:1184-1193(1996).
[4]
FUNCTION IN CELL PROLIFERATION.
PubMed=8657124; DOI=10.1128/MCB.16.4.1509;
Xiong Q., Chan J.L., Zong C.S., Wang L.H.;
"Two chimeric receptors of epidermal growth factor receptor and c-Ros
that differ in their transmembrane domains have opposite effects on
cell growth.";
Mol. Cell. Biol. 16:1509-1518(1996).
[5]
FUNCTION IN STAT3 ACTIVATION.
PubMed=9774423; DOI=10.1074/jbc.273.43.28065;
Zong C.S., Zeng L., Jiang Y., Sadowski H.B., Wang L.H.;
"Stat3 plays an important role in oncogenic Ros- and insulin-like
growth factor I receptor-induced anchorage-independent growth.";
J. Biol. Chem. 273:28065-28072(1998).
[6]
FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTPN6, ENZYME
REGULATION, PHOSPHORYLATION AT TYR-2267, AND MUTAGENESIS OF TYR-2267.
PubMed=11266449; DOI=10.1083/jcb.152.2.325;
Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M.,
Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B.,
Mueller T., Birchmeier C., Boehmer F.D.;
"Negative regulation of Ros receptor tyrosine kinase signaling. An
epithelial function of the SH2 domain protein tyrosine phosphatase
SHP-1.";
J. Cell Biol. 152:325-334(2001).
[7]
FUNCTION IN PI3 KINASE AND STAT3 ACTIVATION.
PubMed=11799110; DOI=10.1074/jbc.M108166200;
Nguyen K.T., Zong C.S., Uttamsingh S., Sachdev P., Bhanot M., Le M.T.,
Chan J.L., Wang L.H.;
"The role of phosphatidylinositol 3-kinase, rho family GTPases, and
STAT3 in Ros-induced cell transformation.";
J. Biol. Chem. 277:11107-11115(2002).
-!- FUNCTION: Orphan receptor tyrosine kinase (RTK) that plays a role
in epithelial cell differentiation and regionalization of the
proximal epididymal epithelium. May activate several downstream
signaling pathways related to cell differentiation, proliferation,
growth and survival including the PI3 kinase-mTOR signaling
pathway. Mediates the phosphorylation of PTPN11, an activator of
this pathway. May also phosphorylate and activate the
transcription factor STAT3 to control anchorage-independent cell
growth. Mediates the phosphorylation and the activation of VAV3, a
guanine nucleotide exchange factor regulating cell morphology. May
activate other downstream signaling proteins including AKT1,
MAPK1, MAPK3, IRS1, and PLCG2. {ECO:0000269|PubMed:11266449,
ECO:0000269|PubMed:11799110, ECO:0000269|PubMed:8657124,
ECO:0000269|PubMed:8675006, ECO:0000269|PubMed:9774423}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Inhibited by dephosphorylation by PTPN6.
{ECO:0000269|PubMed:11266449}.
-!- SUBUNIT: Interacts with PTPN11; may activate the PI3 kinase-mTOR
signaling pathway. Interacts with VAV3; constitutive interaction
mediating VAV3 phosphorylation (By similarity). Interacts with
PTPN6 (via SH2 1 domain); the interaction is direct and promotes
ROS1 dephosphorylation. {ECO:0000250,
ECO:0000269|PubMed:11266449}.
-!- INTERACTION:
P29351:Ptpn6; NbExp=3; IntAct=EBI-7800362, EBI-2620699;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed by epithelial cells of the caput
epididymis (at protein level). {ECO:0000269|PubMed:8675006}.
-!- PTM: Phosphorylated. Probably autophosphorylates. Phosphorylation
at Tyr-2267 and/or Tyr-2327 recruits PTPN11 (By similarity).
Phosphorylation at Tyr-2267 is required for the interaction with
PTPN6 that mediates ROS1 dephosphorylation. Phosphorylation at
Tyr-2267 stimulates the kinase activity and the activation of the
ERK1 signaling cascade. {ECO:0000250,
ECO:0000269|PubMed:11266449}.
-!- DISRUPTION PHENOTYPE: Mice are viable and healthy. Females display
normal fertility while males are sterile due a non-cell autonomous
defect in sperm maturation. It is associated with the absence of
tall columnar epithelial cells with long microvilli in the
proximal part of the caput epididymidis.
{ECO:0000269|PubMed:8675006}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X81650; CAA57310.1; -; mRNA.
EMBL; U15443; AAA50600.1; -; mRNA.
CCDS; CCDS23838.1; -.
RefSeq; NP_035412.2; NM_011282.2.
UniGene; Mm.236163; -.
ProteinModelPortal; Q78DX7; -.
SMR; Q78DX7; -.
IntAct; Q78DX7; 3.
MINT; Q78DX7; -.
STRING; 10090.ENSMUSP00000020045; -.
BindingDB; Q78DX7; -.
ChEMBL; CHEMBL2034802; -.
iPTMnet; Q78DX7; -.
PhosphoSitePlus; Q78DX7; -.
PaxDb; Q78DX7; -.
PRIDE; Q78DX7; -.
Ensembl; ENSMUST00000020045; ENSMUSP00000020045; ENSMUSG00000019893.
GeneID; 19886; -.
KEGG; mmu:19886; -.
UCSC; uc007fbb.1; mouse.
CTD; 6098; -.
MGI; MGI:97999; Ros1.
eggNOG; ENOG410IQAA; Eukaryota.
eggNOG; ENOG410XSTC; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000137937; -.
HOVERGEN; HBG058631; -.
InParanoid; Q78DX7; -.
KO; K05088; -.
OMA; YWLVQDS; -.
OrthoDB; EOG091G003T; -.
PhylomeDB; Q78DX7; -.
TreeFam; TF351636; -.
PRO; PR:Q78DX7; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019893; -.
CleanEx; MM_ROS1; -.
ExpressionAtlas; Q78DX7; baseline and differential.
Genevisible; Q78DX7; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0010966; P:regulation of phosphate transport; IMP:MGI.
GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IDA:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
CDD; cd00063; FN3; 8.
Gene3D; 2.120.10.30; -; 3.
Gene3D; 2.60.40.10; -; 8.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF00041; fn3; 3.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 9.
SMART; SM00135; LY; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50853; FN3; 9.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 2340 Proto-oncogene tyrosine-protein kinase
ROS.
/FTId=PRO_0000278115.
TOPO_DOM 29 1854 Extracellular. {ECO:0000255}.
TRANSMEM 1855 1875 Helical. {ECO:0000255}.
TOPO_DOM 1876 2340 Cytoplasmic. {ECO:0000255}.
DOMAIN 111 206 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 207 295 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 567 667 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 943 1038 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1039 1146 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1442 1549 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1550 1649 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1651 1744 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1745 1846 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1938 2216 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1944 1952 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 2072 2072 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1973 1973 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2267 2267 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11266449}.
MOD_RES 2327 2327 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08922}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 935 935 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1011 1011 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1243 1243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1676 1676 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 2267 2267 Y->F: Abrogates interaction with PTPN6.
{ECO:0000269|PubMed:11266449}.
CONFLICT 27 27 Q -> L (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 109 111 TEL -> QAI (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 329 329 D -> Y (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 419 419 I -> V (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 591 591 A -> P (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 595 595 G -> P (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 631 632 NV -> KL (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 642 645 TVSV -> PFSC (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 656 656 W -> G (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 671 672 PP -> LL (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 830 830 I -> V (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1050 1050 S -> R (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1066 1066 N -> D (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1085 1085 S -> F (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1235 1235 Y -> C (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1276 1276 I -> T (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1371 1371 V -> L (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1428 1429 SA -> FR (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1486 1487 ME -> IK (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1541 1545 EIQGQ -> RFKDK (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1585 1592 RYQLVMSY -> AISWLMSD (in Ref. 2;
AAA50600). {ECO:0000305}.
CONFLICT 1669 1669 W -> R (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1778 1778 T -> S (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1893 1893 N -> S (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 1917 1918 AV -> GI (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 2087 2087 S -> N (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 2118 2118 V -> A (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 2270 2272 LAT -> VPQ (in Ref. 2; AAA50600).
{ECO:0000305}.
CONFLICT 2333 2333 S -> R (in Ref. 2; AAA50600).
{ECO:0000305}.
SEQUENCE 2340 AA; 261967 MW; A3A670B0C4151D7C CRC64;
MKNICWLTLK LVKFVVLGCI IWISVAQSTV LSSCLTSCVT NLGRQLDSGT RYNLSEACIH
GCQFWNSVDQ ETCALKCNDT YATICERESC EVGCSNAEGS YEEEVLESTE LPTAPFASSI
GSHGVTLRWN PANISGVKYI IQWKYAQLPG SWTFTETVSK LSYTVEPLHP FTEYIFRVVW
IFTAQLHLYS PPSPSYRTHP YGVPETAPLI LNMESWSPDT VEVSWAPPHF PGGPILGYNL
RLISKNQKLD SGTQRTSFQF YSTLPNTTYR FSIAAVNEVG EGPEAESTVT TPSPSVQEEE
QWLFLSRKTS LRKRSLKYLV DEAHCLWSDA IHHNITGISV YAQQQVVYFS EGTVIWMKGA
ANMSDVSDLR IFYQGSGLVS SISIDWLYQR MYFIMDKLVY VCELKNCSNL EEITPFSLIA
PQKVVVDSYN GYLFYLLRDG IYRVNLPLPS GRDTKAVRIV ESGTLKDFAV KPQSKRIIYF
NDTMQLFMST FLDGSAFHRV LPWVPLVTVK SFACENNDFL ITDGKAIFQQ DSLSFNEFIV
GCDLSHIEEF GFGNLVIFGS SVQSYPLPGH PQEVSVLFGS REALIQWTPP ALAIGASPSA
WQNWTYEVKV YSQDILEITQ VFSNISGTML NVPELQSSTK YTVSVRASSP KGPGPWSAPS
VGTTLVPATE PPFIMAVKED GLWSKPLCSF GPGEFLSSDV GNVSDMDWYN NSLYYSDTKG
NVYVRPLNGM DISENYHIPS IVGAGALAFE WLGHFLYWAG KTYVIQRQSV LTGHTDIVTH
VKLLVNDMAV DSVGGYLYWT TLYSVESTRL NGESSLVLQA QPWLSGKKVI ALTLDLSDGL
LYWLVQDNQC IHLYTAVLRG WSGGDATITE FAAWSTSEIS QNALMYYSGR LFWINGFRII
TAQEIGQRTS VSVSEPAKFN QFTIIQTSLK PLPGNFSSTP KVIPDPVQES SFRIEGHTSS
FQILWNEPPA VDWGIVFYSV EFSTHSKFLI IEQQSLPIFT VEGLEPYTLF NLSVTPYTYW
GKGQKTSLSF RAPESVPSAP ENPRIFILSS GRYTKKNEVV VEFRWNKPKH ENGVLTKFEI
FYHISKQSGT NRSTEDWMSA SVIPPVMSFQ LEAVSPEYTV AFQVRVFTSK GPGPFSDIVM
SKTSEIKPCP YLISLLGNKI VFLDMDQNQV LWTFSLEGDV STVGYTTDDE MGYFAQGDTL
FLLNLRNHSS SKLFQDALVS DIRVIAVDWI ARHLYFALKA SQNGTQIFNV DLEHKVKSPR
EVKTCKAHTT IISFSIYPLL SRLYWTEVSD LGHQMFYCNI SNHTSQHVLQ PKASNQHGRS
QCSCNVTESE LSGAMTVDTS DPDRPWIYFT KRQEIWAMDL EGCQCWKVIM VPTIPGKRII
SLTVDGEFIY WIMKTKDDAQ IYQAKKGSGA ILSQVKASRS KHILAYSSAL QPFPDKAYLS
LASDMVEATI LYATNTSLTL KLPPVKTNLT WHGITHPTST YLIYYMEANR ANSSDRRHKM
LESQENVARI EGLQPFSMYM IQIAVKNYYS EPLEHLPLGK EIQGQTKSGV PGAVCHINAT
VLSDTSLHVF WTESHKPNGP KESVRYQLVM SYLAPIPETP LRQGEFPSAK LSLLITKLSG
GQLYVMKVLA CHPEEMWCTE SHPVSVNMFD TPEKPSALVP ENTSLQLDWK ARSNVNLTGF
WFELQKWKYN EFYHVKASCS QGPVYVCNIT DLQPYTSYNI RVVVVYTTGE NSSSIPESFK
TKAGVPSKPG IPKLLEGSKN SIQWEKAEDN GSRLMYYTLE VRKGISNDSQ NQSSRWKVVF
NGSCSSICTW RSKNLKGTFQ FRAVAANEIG LGEYSEISED ITLVEDGVWI TETSFILTII
VGIFLVATVP LTFVWHRSLK SHKASKEGLS VLNDNDKELA ELRGLAAGVG LANACYAVHT
VPTQEEIENL PAFPREKLSL RLLLGSGAFG EVYEGTAIDI LGVGSGEIKV AVKTLKKGST
DQEKIEFLKE AHLMSKFNHP NILKQLGVCL LGEPQYIILE LMEGGDLLSY LRKARGTTFH
GPSLTLLDLV ELCVDISKGC VYLEQMHFIH RDLAARNCLV SVKDYTSPRV VKIGDFGLAR
EIYKNDYYRK RGEGLLPVRW MAPENLMDGI FTSQSDVWSF GILVWEILTL GHQPYPAHSN
LDVLNYVQAG GRLEPPRNCP DDLWNLMSQC WAQEPDQRPT FHNIQNQLQL FRNVFLNNVS
HCGEAAPTGG VINKGFEGED DEMVTLNSDD TMPVALMETK NQEGLNYMVL ATKCSQGEGS
YEGPLGPKEL GSCDLKKDKK QPQADKDFCQ EPQVAYGSPG LSEGLNYACL AHSEHGDVSE


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U0978r CLIA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
E0978r ELISA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
E0978h ELISA kit ERBB2,HER2,Homo sapiens,Human,Metastatic lymph node gene 19 protein,MLN 19,MLN19,NEU,NGL,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2,Tyrosin 96T
EIAAB39853 Chicken,Gallus gallus,p60-Src,pp60c-src,Proto-oncogene c-Src,Proto-oncogene tyrosine-protein kinase Src,SRC
EIAAB35720 Chicken,Gallus gallus,Proto-oncogene c-Ros-1,Proto-oncogene tyrosine-protein kinase ROS,ROS1
15-288-22631 Receptor tyrosine-protein kinase erbB-2 - EC 2.7.10.1; p185erbB2; C-erbB-2; NEU proto-oncogene; Tyrosine kinase-type cell surface receptor HER2; MLN 19 Polyclonal 0.05 mg
15-288-22631 Receptor tyrosine-protein kinase erbB-2 - EC 2.7.10.1; p185erbB2; C-erbB-2; NEU proto-oncogene; Tyrosine kinase-type cell surface receptor HER2; MLN 19 Polyclonal 0.1 mg
EH1750 Proto-oncogene tyrosine-protein kinase receptor Ret Elisa Kit 96T
G4700 Proto-oncogene tyrosine-protein kinase receptor Ret (RET), Human, ELISA Kit 96T
CSB-EL019572HU Human Proto-oncogene tyrosine-protein kinase receptor Ret(RET) ELISA kit 96T


 

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