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Q78DX7

- ROS1_MOUSE

UniProt

Q78DX7 - ROS1_MOUSE

Protein

Proto-oncogene tyrosine-protein kinase ROS

Gene

Ros1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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 PLCG2.5 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by dephosphorylation by PTPN6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1973 – 19731ATPPROSITE-ProRule annotation
    Active sitei2072 – 20721Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1944 – 19529ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein phosphatase binding Source: UniProtKB
    3. protein tyrosine kinase activity Source: UniProtKB
    4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell differentiation Source: UniProtKB
    2. cell growth Source: UniProtKB
    3. cell proliferation Source: UniProtKB
    4. columnar/cuboidal epithelial cell development Source: UniProtKB
    5. negative regulation of gene expression Source: MGI
    6. protein phosphorylation Source: UniProtKB
    7. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    8. regulation of phosphate transport Source: MGI
    9. regulation of TOR signaling Source: UniProtKB
    10. spermatogenesis Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene tyrosine-protein kinase ROS (EC:2.7.10.1)
    Alternative name(s):
    Proto-oncogene c-Ros
    Proto-oncogene c-Ros-1
    Receptor tyrosine kinase c-ros oncogene 1
    c-Ros receptor tyrosine kinase
    Gene namesi
    Name:Ros1
    Synonyms:Ros, Ros-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97999. Ros1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2267 – 22671Y → F: Abrogates interaction with PTPN6. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 23402312Proto-oncogene tyrosine-protein kinase ROSPRO_0000278115Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi935 – 9351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1011 – 10111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1243 – 12431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1676 – 16761N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2267 – 22671Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei2327 – 23271Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    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.By similarity1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ78DX7.
    PRIDEiQ78DX7.

    PTM databases

    PhosphoSiteiQ78DX7.

    Expressioni

    Tissue specificityi

    Expressed by epithelial cells of the caput epididymis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ78DX7.
    BgeeiQ78DX7.
    CleanExiMM_ROS1.
    GenevestigatoriQ78DX7.

    Interactioni

    Subunit structurei

    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.By similarity1 Publication

    Protein-protein interaction databases

    MINTiMINT-192643.

    Structurei

    3D structure databases

    ProteinModelPortaliQ78DX7.
    SMRiQ78DX7. Positions 112-180, 203-288, 580-664, 955-1143, 1651-1839, 1927-2268.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 18541826ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1876 – 2340465CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1855 – 187521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 20696Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini207 – 29589Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini567 – 667101Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini943 – 103896Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1039 – 1146108Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1442 – 1549108Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1550 – 1649100Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1651 – 174494Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1745 – 1846102Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1938 – 2216279Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
    Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117362.
    HOGENOMiHOG000137937.
    HOVERGENiHBG058631.
    InParanoidiQ78DX7.
    KOiK05088.
    OMAiYWLVQDS.
    PhylomeDBiQ78DX7.
    TreeFamiTF351636.

    Family and domain databases

    Gene3Di2.120.10.30. 3 hits.
    2.60.40.10. 9 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000033. LDLR_classB_rpt.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00041. fn3. 4 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00060. FN3. 9 hits.
    SM00135. LY. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 5 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50853. FN3. 9 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q78DX7-1 [UniParc]FASTAAdd to Basket

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    MKNICWLTLK LVKFVVLGCI IWISVAQSTV LSSCLTSCVT NLGRQLDSGT     50
    RYNLSEACIH GCQFWNSVDQ ETCALKCNDT YATICERESC EVGCSNAEGS 100
    YEEEVLESTE LPTAPFASSI GSHGVTLRWN PANISGVKYI IQWKYAQLPG 150
    SWTFTETVSK LSYTVEPLHP FTEYIFRVVW IFTAQLHLYS PPSPSYRTHP 200
    YGVPETAPLI LNMESWSPDT VEVSWAPPHF PGGPILGYNL RLISKNQKLD 250
    SGTQRTSFQF YSTLPNTTYR FSIAAVNEVG EGPEAESTVT TPSPSVQEEE 300
    QWLFLSRKTS LRKRSLKYLV DEAHCLWSDA IHHNITGISV YAQQQVVYFS 350
    EGTVIWMKGA ANMSDVSDLR IFYQGSGLVS SISIDWLYQR MYFIMDKLVY 400
    VCELKNCSNL EEITPFSLIA PQKVVVDSYN GYLFYLLRDG IYRVNLPLPS 450
    GRDTKAVRIV ESGTLKDFAV KPQSKRIIYF NDTMQLFMST FLDGSAFHRV 500
    LPWVPLVTVK SFACENNDFL ITDGKAIFQQ DSLSFNEFIV GCDLSHIEEF 550
    GFGNLVIFGS SVQSYPLPGH PQEVSVLFGS REALIQWTPP ALAIGASPSA 600
    WQNWTYEVKV YSQDILEITQ VFSNISGTML NVPELQSSTK YTVSVRASSP 650
    KGPGPWSAPS VGTTLVPATE PPFIMAVKED GLWSKPLCSF GPGEFLSSDV 700
    GNVSDMDWYN NSLYYSDTKG NVYVRPLNGM DISENYHIPS IVGAGALAFE 750
    WLGHFLYWAG KTYVIQRQSV LTGHTDIVTH VKLLVNDMAV DSVGGYLYWT 800
    TLYSVESTRL NGESSLVLQA QPWLSGKKVI ALTLDLSDGL LYWLVQDNQC 850
    IHLYTAVLRG WSGGDATITE FAAWSTSEIS QNALMYYSGR LFWINGFRII 900
    TAQEIGQRTS VSVSEPAKFN QFTIIQTSLK PLPGNFSSTP KVIPDPVQES 950
    SFRIEGHTSS FQILWNEPPA VDWGIVFYSV EFSTHSKFLI IEQQSLPIFT 1000
    VEGLEPYTLF NLSVTPYTYW GKGQKTSLSF RAPESVPSAP ENPRIFILSS 1050
    GRYTKKNEVV VEFRWNKPKH ENGVLTKFEI FYHISKQSGT NRSTEDWMSA 1100
    SVIPPVMSFQ LEAVSPEYTV AFQVRVFTSK GPGPFSDIVM SKTSEIKPCP 1150
    YLISLLGNKI VFLDMDQNQV LWTFSLEGDV STVGYTTDDE MGYFAQGDTL 1200
    FLLNLRNHSS SKLFQDALVS DIRVIAVDWI ARHLYFALKA SQNGTQIFNV 1250
    DLEHKVKSPR EVKTCKAHTT IISFSIYPLL SRLYWTEVSD LGHQMFYCNI 1300
    SNHTSQHVLQ PKASNQHGRS QCSCNVTESE LSGAMTVDTS DPDRPWIYFT 1350
    KRQEIWAMDL EGCQCWKVIM VPTIPGKRII SLTVDGEFIY WIMKTKDDAQ 1400
    IYQAKKGSGA ILSQVKASRS KHILAYSSAL QPFPDKAYLS LASDMVEATI 1450
    LYATNTSLTL KLPPVKTNLT WHGITHPTST YLIYYMEANR ANSSDRRHKM 1500
    LESQENVARI EGLQPFSMYM IQIAVKNYYS EPLEHLPLGK EIQGQTKSGV 1550
    PGAVCHINAT VLSDTSLHVF WTESHKPNGP KESVRYQLVM SYLAPIPETP 1600
    LRQGEFPSAK LSLLITKLSG GQLYVMKVLA CHPEEMWCTE SHPVSVNMFD 1650
    TPEKPSALVP ENTSLQLDWK ARSNVNLTGF WFELQKWKYN EFYHVKASCS 1700
    QGPVYVCNIT DLQPYTSYNI RVVVVYTTGE NSSSIPESFK TKAGVPSKPG 1750
    IPKLLEGSKN SIQWEKAEDN GSRLMYYTLE VRKGISNDSQ NQSSRWKVVF 1800
    NGSCSSICTW RSKNLKGTFQ FRAVAANEIG LGEYSEISED ITLVEDGVWI 1850
    TETSFILTII VGIFLVATVP LTFVWHRSLK SHKASKEGLS VLNDNDKELA 1900
    ELRGLAAGVG LANACYAVHT VPTQEEIENL PAFPREKLSL RLLLGSGAFG 1950
    EVYEGTAIDI LGVGSGEIKV AVKTLKKGST DQEKIEFLKE AHLMSKFNHP 2000
    NILKQLGVCL LGEPQYIILE LMEGGDLLSY LRKARGTTFH GPSLTLLDLV 2050
    ELCVDISKGC VYLEQMHFIH RDLAARNCLV SVKDYTSPRV VKIGDFGLAR 2100
    EIYKNDYYRK RGEGLLPVRW MAPENLMDGI FTSQSDVWSF GILVWEILTL 2150
    GHQPYPAHSN LDVLNYVQAG GRLEPPRNCP DDLWNLMSQC WAQEPDQRPT 2200
    FHNIQNQLQL FRNVFLNNVS HCGEAAPTGG VINKGFEGED DEMVTLNSDD 2250
    TMPVALMETK NQEGLNYMVL ATKCSQGEGS YEGPLGPKEL GSCDLKKDKK 2300
    QPQADKDFCQ EPQVAYGSPG LSEGLNYACL AHSEHGDVSE 2340
    Length:2,340
    Mass (Da):261,967
    Last modified:July 5, 2004 - v1
    Checksum:iA3A670B0C4151D7C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271Q → L in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti109 – 1113TEL → QAI in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti329 – 3291D → Y in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti419 – 4191I → V in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti591 – 5911A → P in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti595 – 5951G → P in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti631 – 6322NV → KL in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti642 – 6454TVSV → PFSC in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti656 – 6561W → G in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti671 – 6722PP → LL in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti830 – 8301I → V in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1050 – 10501S → R in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1066 – 10661N → D in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1085 – 10851S → F in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1235 – 12351Y → C in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1276 – 12761I → T in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1371 – 13711V → L in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1428 – 14292SA → FR in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1486 – 14872ME → IK in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1541 – 15455EIQGQ → RFKDK in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1585 – 15928RYQLVMSY → AISWLMSD in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1669 – 16691W → R in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1778 – 17781T → S in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1893 – 18931N → S in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti1917 – 19182AV → GI in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti2087 – 20871S → N in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti2118 – 21181V → A in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti2270 – 22723LAT → VPQ in AAA50600. (PubMed:8544427)Curated
    Sequence conflicti2333 – 23331S → R in AAA50600. (PubMed:8544427)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81650 mRNA. Translation: CAA57310.1.
    U15443 mRNA. Translation: AAA50600.1.
    CCDSiCCDS23838.1.
    RefSeqiNP_035412.2. NM_011282.2.
    UniGeneiMm.236163.

    Genome annotation databases

    EnsembliENSMUST00000020045; ENSMUSP00000020045; ENSMUSG00000019893.
    GeneIDi19886.
    KEGGimmu:19886.
    UCSCiuc007fbb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81650 mRNA. Translation: CAA57310.1 .
    U15443 mRNA. Translation: AAA50600.1 .
    CCDSi CCDS23838.1.
    RefSeqi NP_035412.2. NM_011282.2.
    UniGenei Mm.236163.

    3D structure databases

    ProteinModelPortali Q78DX7.
    SMRi Q78DX7. Positions 112-180, 203-288, 580-664, 955-1143, 1651-1839, 1927-2268.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-192643.

    Chemistry

    ChEMBLi CHEMBL2034802.

    PTM databases

    PhosphoSitei Q78DX7.

    Proteomic databases

    PaxDbi Q78DX7.
    PRIDEi Q78DX7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020045 ; ENSMUSP00000020045 ; ENSMUSG00000019893 .
    GeneIDi 19886.
    KEGGi mmu:19886.
    UCSCi uc007fbb.1. mouse.

    Organism-specific databases

    CTDi 6098.
    MGIi MGI:97999. Ros1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117362.
    HOGENOMi HOG000137937.
    HOVERGENi HBG058631.
    InParanoidi Q78DX7.
    KOi K05088.
    OMAi YWLVQDS.
    PhylomeDBi Q78DX7.
    TreeFami TF351636.

    Miscellaneous databases

    NextBioi 297396.
    PROi Q78DX7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q78DX7.
    Bgeei Q78DX7.
    CleanExi MM_ROS1.
    Genevestigatori Q78DX7.

    Family and domain databases

    Gene3Di 2.120.10.30. 3 hits.
    2.60.40.10. 9 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000033. LDLR_classB_rpt.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00041. fn3. 4 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00060. FN3. 9 hits.
    SM00135. LY. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 5 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50853. FN3. 9 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Biochemical and functional characterization of the murine ros protooncogene."
      Riethmacher D., Langholz O., Godecke S., Sachs M., Birchmeier C.
      Oncogene 9:3617-3626(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NMRI.
      Tissue: Intestine.
    2. "Cloning of mouse c-ros renal cDNA, its role in development and relationship to extracellular matrix glycoproteins."
      Kanwar Y.S., Liu Z.Z., Kumar A., Wada J., Carone F.A.
      Kidney Int. 48:1646-1659(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1.
      Tissue: Kidney.
    3. "The c-ros tyrosine kinase receptor controls regionalization and differentiation of epithelial cells in the epididymis."
      Sonnenberg-Riethmacher E., Walter B., Riethmacher D., Goedecke S., Birchmeier C.
      Genes Dev. 10:1184-1193(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN EPITHELIUM DIFFERENTIATION, TISSUE SPECIFICITY.
    4. "Two chimeric receptors of epidermal growth factor receptor and c-Ros that differ in their transmembrane domains have opposite effects on cell growth."
      Xiong Q., Chan J.L., Zong C.S., Wang L.H.
      Mol. Cell. Biol. 16:1509-1518(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION.
    5. "Stat3 plays an important role in oncogenic Ros- and insulin-like growth factor I receptor-induced anchorage-independent growth."
      Zong C.S., Zeng L., Jiang Y., Sadowski H.B., Wang L.H.
      J. Biol. Chem. 273:28065-28072(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STAT3 ACTIVATION.
    6. "Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1."
      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.
      J. Cell Biol. 152:325-334(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTPN6, ENZYME REGULATION, PHOSPHORYLATION AT TYR-2267, MUTAGENESIS OF TYR-2267.
    7. "The role of phosphatidylinositol 3-kinase, rho family GTPases, and STAT3 in Ros-induced cell transformation."
      Nguyen K.T., Zong C.S., Uttamsingh S., Sachdev P., Bhanot M., Le M.T., Chan J.L., Wang L.H.
      J. Biol. Chem. 277:11107-11115(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PI3 KINASE AND STAT3 ACTIVATION.

    Entry informationi

    Entry nameiROS1_MOUSE
    AccessioniPrimary (citable) accession number: Q78DX7
    Secondary accession number(s): Q60705
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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