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Q78DX7

- ROS1_MOUSE

UniProt

Q78DX7 - ROS1_MOUSE

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Protein

Proto-oncogene tyrosine-protein kinase ROS

Gene
Ros1, Ros, Ros-1
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.

Enzyme regulationi

Inhibited by dephosphorylation by PTPN6.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1973 – 19731ATP By similarity
Active sitei2072 – 20721Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1944 – 19529ATP By similarity

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
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 18541826Extracellular Reviewed predictionAdd
BLAST
Transmembranei1855 – 187521Helical; Reviewed predictionAdd
BLAST
Topological domaini1876 – 2340465Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
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 – 2828 Reviewed predictionAdd
BLAST
Chaini29 – 23402312Proto-oncogene tyrosine-protein kinase ROSPRO_0000278115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi334 – 3341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi362 – 3621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi935 – 9351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1011 – 10111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1243 – 12431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1676 – 16761N-linked (GlcNAc...) Reviewed prediction
Modified residuei2267 – 22671Phosphotyrosine; by autocatalysis1 Publication
Modified residuei2327 – 23271Phosphotyrosine; by autocatalysis By 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.1 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.1 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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271Q → L in AAA50600. 1 Publication
Sequence conflicti109 – 1113TEL → QAI in AAA50600. 1 Publication
Sequence conflicti329 – 3291D → Y in AAA50600. 1 Publication
Sequence conflicti419 – 4191I → V in AAA50600. 1 Publication
Sequence conflicti591 – 5911A → P in AAA50600. 1 Publication
Sequence conflicti595 – 5951G → P in AAA50600. 1 Publication
Sequence conflicti631 – 6322NV → KL in AAA50600. 1 Publication
Sequence conflicti642 – 6454TVSV → PFSC in AAA50600. 1 Publication
Sequence conflicti656 – 6561W → G in AAA50600. 1 Publication
Sequence conflicti671 – 6722PP → LL in AAA50600. 1 Publication
Sequence conflicti830 – 8301I → V in AAA50600. 1 Publication
Sequence conflicti1050 – 10501S → R in AAA50600. 1 Publication
Sequence conflicti1066 – 10661N → D in AAA50600. 1 Publication
Sequence conflicti1085 – 10851S → F in AAA50600. 1 Publication
Sequence conflicti1235 – 12351Y → C in AAA50600. 1 Publication
Sequence conflicti1276 – 12761I → T in AAA50600. 1 Publication
Sequence conflicti1371 – 13711V → L in AAA50600. 1 Publication
Sequence conflicti1428 – 14292SA → FR in AAA50600. 1 Publication
Sequence conflicti1486 – 14872ME → IK in AAA50600. 1 Publication
Sequence conflicti1541 – 15455EIQGQ → RFKDK in AAA50600. 1 Publication
Sequence conflicti1585 – 15928RYQLVMSY → AISWLMSD in AAA50600. 1 Publication
Sequence conflicti1669 – 16691W → R in AAA50600. 1 Publication
Sequence conflicti1778 – 17781T → S in AAA50600. 1 Publication
Sequence conflicti1893 – 18931N → S in AAA50600. 1 Publication
Sequence conflicti1917 – 19182AV → GI in AAA50600. 1 Publication
Sequence conflicti2087 – 20871S → N in AAA50600. 1 Publication
Sequence conflicti2118 – 21181V → A in AAA50600. 1 Publication
Sequence conflicti2270 – 22723LAT → VPQ in AAA50600. 1 Publication
Sequence conflicti2333 – 23331S → R in AAA50600. 1 Publication

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: July 9, 2014
This is version 93 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

Similar proteinsi