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Q78DX7

- ROS1_MOUSE

UniProt

Q78DX7 - ROS1_MOUSE

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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

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. peptidyl-tyrosine phosphorylation Source: GOC
  7. protein phosphorylation Source: UniProtKB
  8. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  9. regulation of phosphate transport Source: MGI
  10. regulation of TOR signaling Source: UniProtKB
  11. spermatogenesis Source: UniProtKB
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ78DX7.
CleanExiMM_ROS1.
ExpressionAtlasiQ78DX7. differential.
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 203-288, 567-667, 955-1143, 1705-1839, 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.
GeneTreeiENSGT00760000118818.
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

« Hide

        10         20         30         40         50
MKNICWLTLK LVKFVVLGCI IWISVAQSTV LSSCLTSCVT NLGRQLDSGT
60 70 80 90 100
RYNLSEACIH GCQFWNSVDQ ETCALKCNDT YATICERESC EVGCSNAEGS
110 120 130 140 150
YEEEVLESTE LPTAPFASSI GSHGVTLRWN PANISGVKYI IQWKYAQLPG
160 170 180 190 200
SWTFTETVSK LSYTVEPLHP FTEYIFRVVW IFTAQLHLYS PPSPSYRTHP
210 220 230 240 250
YGVPETAPLI LNMESWSPDT VEVSWAPPHF PGGPILGYNL RLISKNQKLD
260 270 280 290 300
SGTQRTSFQF YSTLPNTTYR FSIAAVNEVG EGPEAESTVT TPSPSVQEEE
310 320 330 340 350
QWLFLSRKTS LRKRSLKYLV DEAHCLWSDA IHHNITGISV YAQQQVVYFS
360 370 380 390 400
EGTVIWMKGA ANMSDVSDLR IFYQGSGLVS SISIDWLYQR MYFIMDKLVY
410 420 430 440 450
VCELKNCSNL EEITPFSLIA PQKVVVDSYN GYLFYLLRDG IYRVNLPLPS
460 470 480 490 500
GRDTKAVRIV ESGTLKDFAV KPQSKRIIYF NDTMQLFMST FLDGSAFHRV
510 520 530 540 550
LPWVPLVTVK SFACENNDFL ITDGKAIFQQ DSLSFNEFIV GCDLSHIEEF
560 570 580 590 600
GFGNLVIFGS SVQSYPLPGH PQEVSVLFGS REALIQWTPP ALAIGASPSA
610 620 630 640 650
WQNWTYEVKV YSQDILEITQ VFSNISGTML NVPELQSSTK YTVSVRASSP
660 670 680 690 700
KGPGPWSAPS VGTTLVPATE PPFIMAVKED GLWSKPLCSF GPGEFLSSDV
710 720 730 740 750
GNVSDMDWYN NSLYYSDTKG NVYVRPLNGM DISENYHIPS IVGAGALAFE
760 770 780 790 800
WLGHFLYWAG KTYVIQRQSV LTGHTDIVTH VKLLVNDMAV DSVGGYLYWT
810 820 830 840 850
TLYSVESTRL NGESSLVLQA QPWLSGKKVI ALTLDLSDGL LYWLVQDNQC
860 870 880 890 900
IHLYTAVLRG WSGGDATITE FAAWSTSEIS QNALMYYSGR LFWINGFRII
910 920 930 940 950
TAQEIGQRTS VSVSEPAKFN QFTIIQTSLK PLPGNFSSTP KVIPDPVQES
960 970 980 990 1000
SFRIEGHTSS FQILWNEPPA VDWGIVFYSV EFSTHSKFLI IEQQSLPIFT
1010 1020 1030 1040 1050
VEGLEPYTLF NLSVTPYTYW GKGQKTSLSF RAPESVPSAP ENPRIFILSS
1060 1070 1080 1090 1100
GRYTKKNEVV VEFRWNKPKH ENGVLTKFEI FYHISKQSGT NRSTEDWMSA
1110 1120 1130 1140 1150
SVIPPVMSFQ LEAVSPEYTV AFQVRVFTSK GPGPFSDIVM SKTSEIKPCP
1160 1170 1180 1190 1200
YLISLLGNKI VFLDMDQNQV LWTFSLEGDV STVGYTTDDE MGYFAQGDTL
1210 1220 1230 1240 1250
FLLNLRNHSS SKLFQDALVS DIRVIAVDWI ARHLYFALKA SQNGTQIFNV
1260 1270 1280 1290 1300
DLEHKVKSPR EVKTCKAHTT IISFSIYPLL SRLYWTEVSD LGHQMFYCNI
1310 1320 1330 1340 1350
SNHTSQHVLQ PKASNQHGRS QCSCNVTESE LSGAMTVDTS DPDRPWIYFT
1360 1370 1380 1390 1400
KRQEIWAMDL EGCQCWKVIM VPTIPGKRII SLTVDGEFIY WIMKTKDDAQ
1410 1420 1430 1440 1450
IYQAKKGSGA ILSQVKASRS KHILAYSSAL QPFPDKAYLS LASDMVEATI
1460 1470 1480 1490 1500
LYATNTSLTL KLPPVKTNLT WHGITHPTST YLIYYMEANR ANSSDRRHKM
1510 1520 1530 1540 1550
LESQENVARI EGLQPFSMYM IQIAVKNYYS EPLEHLPLGK EIQGQTKSGV
1560 1570 1580 1590 1600
PGAVCHINAT VLSDTSLHVF WTESHKPNGP KESVRYQLVM SYLAPIPETP
1610 1620 1630 1640 1650
LRQGEFPSAK LSLLITKLSG GQLYVMKVLA CHPEEMWCTE SHPVSVNMFD
1660 1670 1680 1690 1700
TPEKPSALVP ENTSLQLDWK ARSNVNLTGF WFELQKWKYN EFYHVKASCS
1710 1720 1730 1740 1750
QGPVYVCNIT DLQPYTSYNI RVVVVYTTGE NSSSIPESFK TKAGVPSKPG
1760 1770 1780 1790 1800
IPKLLEGSKN SIQWEKAEDN GSRLMYYTLE VRKGISNDSQ NQSSRWKVVF
1810 1820 1830 1840 1850
NGSCSSICTW RSKNLKGTFQ FRAVAANEIG LGEYSEISED ITLVEDGVWI
1860 1870 1880 1890 1900
TETSFILTII VGIFLVATVP LTFVWHRSLK SHKASKEGLS VLNDNDKELA
1910 1920 1930 1940 1950
ELRGLAAGVG LANACYAVHT VPTQEEIENL PAFPREKLSL RLLLGSGAFG
1960 1970 1980 1990 2000
EVYEGTAIDI LGVGSGEIKV AVKTLKKGST DQEKIEFLKE AHLMSKFNHP
2010 2020 2030 2040 2050
NILKQLGVCL LGEPQYIILE LMEGGDLLSY LRKARGTTFH GPSLTLLDLV
2060 2070 2080 2090 2100
ELCVDISKGC VYLEQMHFIH RDLAARNCLV SVKDYTSPRV VKIGDFGLAR
2110 2120 2130 2140 2150
EIYKNDYYRK RGEGLLPVRW MAPENLMDGI FTSQSDVWSF GILVWEILTL
2160 2170 2180 2190 2200
GHQPYPAHSN LDVLNYVQAG GRLEPPRNCP DDLWNLMSQC WAQEPDQRPT
2210 2220 2230 2240 2250
FHNIQNQLQL FRNVFLNNVS HCGEAAPTGG VINKGFEGED DEMVTLNSDD
2260 2270 2280 2290 2300
TMPVALMETK NQEGLNYMVL ATKCSQGEGS YEGPLGPKEL GSCDLKKDKK
2310 2320 2330 2340
QPQADKDFCQ EPQVAYGSPG LSEGLNYACL AHSEHGDVSE
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 203-288, 567-667, 955-1143, 1705-1839, 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 ENSGT00760000118818.
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

Bgeei Q78DX7.
CleanExi MM_ROS1.
ExpressionAtlasi Q78DX7. differential.
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 29, 2014
This is version 95 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

Dasty 3