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C-kit receptor tyrosine kinase (KIT proto-oncogene receptor tyrosine kinase) (Kit oncogene) (V-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, isoform CRA_a)

 Q63116_RAT              Unreviewed;       978 AA.
Q63116;
01-NOV-1996, integrated into UniProtKB/TrEMBL.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 156.
SubName: Full=C-kit receptor tyrosine kinase {ECO:0000313|EMBL:BAA02094.1};
SubName: Full=KIT proto-oncogene receptor tyrosine kinase {ECO:0000313|Ensembl:ENSRNOP00000003050};
SubName: Full=Kit oncogene {ECO:0000313|EMBL:ABX45067.1};
SubName: Full=V-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, isoform CRA_a {ECO:0000313|EMBL:EDL89921.1};
Name=Kit {ECO:0000313|EMBL:EDL89921.1,
ECO:0000313|Ensembl:ENSRNOP00000003050, ECO:0000313|RGD:620568};
Synonyms=KIT {ECO:0000313|EMBL:ABX45067.1};
ORFNames=rCG_56893 {ECO:0000313|EMBL:EDL89921.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000313|EMBL:BAA02094.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Sprague-Dawley {ECO:0000313|EMBL:BAA02094.1};
PubMed=1912577;
Tsujimura T., Hirota S., Nomura S., Niwa Y., Yamazaki M., Tono T.,
Morii E., Kim H., Kondo K., Nishimune Y., Kitamura Y.;
"Characterization of Ws mutant allele of rats: a 12-base deletion in
tyrosine kinase domain of c-kit gene.";
Blood 78:1942-1946(1991).
[2] {ECO:0000313|Ensembl:ENSRNOP00000003050, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003050,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3] {ECO:0000313|EMBL:EDL89921.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL89921.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[4] {ECO:0000313|EMBL:EDL89921.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL89921.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:ABX45067.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ACI {ECO:0000313|EMBL:ABX45067.1}, and
BN {ECO:0000313|EMBL:ABX45068.1};
TISSUE=Lung {ECO:0000313|EMBL:ABX45067.1};
Lachel C.M., Fisher K.W., Shull J.D.;
"Characterization of Renag1 Candidates.";
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000213|PubMed:22673903}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7] {ECO:0000313|Ensembl:ENSRNOP00000003050}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003050};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00701269}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000311};
Single-pass type I membrane protein
{ECO:0000256|RuleBase:RU000311}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000256|RuleBase:RU000311}.
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EMBL; AABR07014877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07014878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07014879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; EU247827; ABX45067.1; -; mRNA.
EMBL; EU247828; ABX45068.1; -; mRNA.
EMBL; D12524; BAA02094.1; -; mRNA.
EMBL; CH473981; EDL89921.1; -; Genomic_DNA.
PIR; A49814; A49814.
RefSeq; NP_071600.1; NM_022264.1.
UniGene; Rn.54004; -.
STRING; 10116.ENSRNOP00000003050; -.
Ensembl; ENSRNOT00000003050; ENSRNOP00000003050; ENSRNOG00000002227.
GeneID; 64030; -.
KEGG; rno:64030; -.
CTD; 3815; -.
RGD; 620568; Kit.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112008; -.
HOVERGEN; HBG004335; -.
KO; K05091; -.
OMA; PTFKQIV; -.
OrthoDB; EOG091G01TL; -.
TreeFam; TF325768; -.
Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-1433559; Regulation of KIT signaling.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Proteomes; UP000002494; Chromosome 14.
Bgee; ENSRNOG00000002227; -.
GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; IEA:InterPro.
GO; GO:0005020; F:stem cell factor receptor activity; IEA:Ensembl.
GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0002371; P:dendritic cell cytokine production; IEA:Ensembl.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0050673; P:epithelial cell proliferation; IMP:RGD.
GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
GO; GO:0038162; P:erythropoietin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0038093; P:Fc receptor signaling pathway; IEA:Ensembl.
GO; GO:0008354; P:germ cell migration; IMP:RGD.
GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
GO; GO:0035701; P:hematopoietic stem cell migration; IEA:Ensembl.
GO; GO:0002327; P:immature B cell differentiation; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0002551; P:mast cell chemotaxis; IEA:Ensembl.
GO; GO:0032762; P:mast cell cytokine production; IEA:Ensembl.
GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
GO; GO:0060374; P:mast cell differentiation; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0097326; P:melanocyte adhesion; IEA:Ensembl.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0097324; P:melanocyte migration; IEA:Ensembl.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:1904343; P:positive regulation of colon smooth muscle contraction; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:RGD.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:RGD.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IMP:RGD.
GO; GO:0120072; P:positive regulation of pyloric antrum smooth muscle contraction; IMP:RGD.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; IMP:RGD.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:1904251; P:regulation of bile acid metabolic process; IMP:RGD.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0048103; P:somatic stem cell division; IMP:RGD.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:RGD.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IMP:RGD.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
GO; GO:0043586; P:tongue development; IEP:RGD.
GO; GO:0008542; P:visual learning; IMP:RGD.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR027263; SCGF_receptor.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500951; SCGF_recepter; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
ATP-binding {ECO:0000256|PIRSR:PIRSR500951-2,
ECO:0000256|SAAS:SAAS00708816};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Disulfide bond {ECO:0000256|SAAS:SAAS00803457};
Immunoglobulin domain {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00442402};
Kinase {ECO:0000256|SAAS:SAAS00582553};
Magnesium {ECO:0000256|PIRSR:PIRSR500951-1};
Membrane {ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|PIRSR:PIRSR500951-1};
Nucleotide-binding {ECO:0000256|PIRSR:PIRSR500951-2,
ECO:0000256|SAAS:SAAS00708816};
Receptor {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00600436, ECO:0000313|EMBL:BAA02094.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Repeat {ECO:0000256|SAAS:SAAS00457685};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|SAAS:SAAS00582553};
Transmembrane {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00582553}.
SIGNAL 1 25 {ECO:0000256|SAM:SignalP}.
CHAIN 26 978 {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5010844889.
TRANSMEM 523 550 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 37 97 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 212 310 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 591 938 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
NP_BIND 598 605 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
NP_BIND 673 679 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
METAL 570 570 Magnesium.
{ECO:0000256|PIRSR:PIRSR500951-1}.
METAL 798 798 Magnesium.
{ECO:0000256|PIRSR:PIRSR500951-1}.
METAL 811 811 Magnesium.
{ECO:0000256|PIRSR:PIRSR500951-1}.
BINDING 625 625 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
BINDING 797 797 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
SITE 937 937 Important for interaction with
phosphotyrosine-binding proteins.
{ECO:0000256|PIRSR:PIRSR500951-3}.
SEQUENCE 978 AA; 109342 MW; 0958C33F19889051 CRC64;
MRGARGAWDL LCVLLVLLRG QTGTSQPSAS PGEPSPPSIQ PAQSELIVEA GDTIRLTCTD
PAFVKWTFEI LDVRIENKQS EWIREKAEAT HTGKYTCVSG SGLRSSIYVF VRDPAVLFLV
GLPLFGKEDN DALVRCPLTD PQVSNYSLIE CDGKSLPTDL KFVPNPKAGI TIKNVKRAYH
RLCIRCAAQR EGKWMRSDKF TLKVRAAIKA IPVVSVPETS HLLKEGDTFT VICTIKDVST
SVDSMWIKLN PQPQSKAQVK RNSWHQGDFN YERQETLTIS SARVNDSGVF MCYANNTFGS
ANVTTTLKVV EKGFINIFPV KNTTVFVTDG ENVDLVVEFE AYPKPEHQQW IYMNRTPTNR
GEDYVKSDNQ SNIRYVNELR LTRLKGTEGG TYTFLVSNSD VSASVTFDVY VNTKPEILTY
DRLMNGRLQC VAAGFPEPTI DWYFCTGAEQ RCTVPVPPVD VQIQNASVSP FGKLVVQSSI
DSSVFRHNGT VECKASNAVG KSSAFFNFAF KGNSKEQIQP HTLFTPLLIG FVVTAGLMGI
IVMVLAYKYL QKPMYEVQWK VVEEINGNNY VYIDPTQLPY DHKWEFPRNR LSFGKTLGAG
AFGKVVEATA YGLIKSDAAM TVAVKMLKPS AHLTEREALM SELKVLSYLG NHMNIVNLLG
ACTVGGPTLV ITEYCCYGDL LNFLRRKRDS FIFSKQEEQA DAALYKNLLH SKESSCDSSN
EYMDMKPGVS YVVPTKTDKR RSARIDSYIE RDVTPAIMED DELALDLEDL LSFSYQVAKG
MAFLASKNCI HRDLAARNIL LTHGRITKIC DFGLARDIRN DSNYVVKGNA RLPVKWMAPE
SIFNCVYTFE SDVWSYGIFL WELFSLGSSP YPGMPVDSKF YKMIKEGFRM LSPEHAPAAM
YEVMKTCWDA DPLKRPTFKQ VVQLIEKQIS DSSKHIYSNL ANCNPNPENP VVVDHSVRVN
SVGSSTSSTQ PLLVHEDA


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E0978h ELISA 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,Tyrosine kin 96T
CSB-EL012375CH Chicken v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog (KIT) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL012375BO Bovine v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog (KIT) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL012375GO Goat v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog (KIT) ELISA kit, Species Goat, Sample Type serum, plasma 96T
U0978h CLIA 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,Tyrosine kina 96T
EIAAB14715 Feline encephalitis virus-related kinase FER,FER,Fujinami poultry sarcoma_Feline sarcoma-related protein Fer,Homo sapiens,Human,p94-Fer,Proto-oncogene c-Fer,TYK3,Tyrosine kinase 3,Tyrosine-protein kin
E0978m ELISA Erbb2,Kiaa3023,Mouse,Mus musculus,Neu,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2 96T
U0978m CLIA Erbb2,Kiaa3023,Mouse,Mus musculus,Neu,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2 96T
E0978m ELISA kit Erbb2,Kiaa3023,Mouse,Mus musculus,Neu,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2 96T


 

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