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Protein

Proto-oncogene tyrosine-protein kinase ROS

Gene

ROS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 PLCG2.2 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by dephosphorylation by PTPN6.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1980ATPCurated1
Active sitei2079Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1951 – 1959ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein phosphatase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00597-MONOMER.
BRENDAi2.7.10.1. 2681.
SignaLinkiP08922.
SIGNORiP08922.

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:MCF3, ROS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10261. ROS1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 1859ExtracellularSequence analysisAdd BLAST1832
Transmembranei1860 – 1882HelicalSequence analysisAdd BLAST23
Topological domaini1883 – 2347CytoplasmicSequence analysisAdd BLAST465

GO - Cellular componenti

  • cell surface Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: ProtInc
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving ROS1 is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which is localized to the Golgi and has a constitutive receptor tyrosine kinase activity. A SLC34A2-ROS1 chimeric protein produced in non-small cell lung cancer cells also retains a constitutive kinase activity. A third type of chimeric protein CD74-ROS1 was also identified in those cells.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1980K → M: Loss of kinase activity. 1 Publication1
Mutagenesisi2274Y → F: Loss of phosphorylation at Y-2274 and loss of interaction with PTPN11. 1 Publication1
Mutagenesisi2334Y → F: Loss of phosphorylation at Y-2334 and loss of interaction with PTPN11. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1852 – 1853Breakpoint for translocation to form SLC34A2-ROS1 and CD74-ROS1 fusion proteins2
Sitei1880 – 1881Breakpoint for translocation to form GOPC-ROS1 fusion protein2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi6098.
OpenTargetsiENSG00000047936.
PharmGKBiPA34633.

Chemistry databases

ChEMBLiCHEMBL5568.
GuidetoPHARMACOLOGYi1840.

Polymorphism and mutation databases

BioMutaiROS1.
DMDMi126302596.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001672228 – 2347Proto-oncogene tyrosine-protein kinase ROSAdd BLAST2320

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Glycosylationi123N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi352N-linked (GlcNAc...)Sequence analysis1
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1
Glycosylationi471N-linked (GlcNAc...)Sequence analysis1
Glycosylationi607N-linked (GlcNAc...)Sequence analysis1
Glycosylationi628N-linked (GlcNAc...)Sequence analysis1
Glycosylationi706N-linked (GlcNAc...)Sequence analysis1
Glycosylationi714N-linked (GlcNAc...)Sequence analysis1
Glycosylationi732N-linked (GlcNAc...)Sequence analysis1
Glycosylationi939N-linked (GlcNAc...)Sequence analysis1
Glycosylationi961N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1015N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1087N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1090N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1095N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1211N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1272N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1330N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1461N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1474N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1499N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1565N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1669N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1715N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1738N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1808N-linked (GlcNAc...)Sequence analysis1
Modified residuei2274Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei2334Phosphotyrosine; by autocatalysis1 Publication1

Post-translational modificationi

Phosphorylated. Probably autophosphorylates. Phosphorylation at Tyr-2274 is required for the interaction with PTPN6 that mediates ROS1 dephosphorylation (By similarity). Phosphorylation at Tyr-2274 stimulates the kinase activity and the activation of the ERK1 signaling cascade (By similarity). Phosphorylation at Tyr-2274 and/or Tyr-2334 recruits PTPN11.By similarity1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP08922.
PaxDbiP08922.
PeptideAtlasiP08922.
PRIDEiP08922.

PTM databases

iPTMnetiP08922.
PhosphoSitePlusiP08922.

Expressioni

Tissue specificityi

Expressed in brain. Expression is increased in primary gliomas.1 Publication

Gene expression databases

BgeeiENSG00000047936.
CleanExiHS_ROS1.
ExpressionAtlasiP08922. baseline and differential.
GenevisibleiP08922. HS.

Organism-specific databases

HPAiHPA049098.

Interactioni

Subunit structurei

Interacts with PTPN6 (via SH2 1 domain); the interaction is direct and promotes ROS1 dephosphorylation (By similarity). Interacts with PTPN11; may activate the PI3 kinase-mTOR signaling pathway. Interacts with VAV3; constitutive interaction mediating VAV3 phosphorylation.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN1P180313EBI-7371065,EBI-968788
PTPN6P293502EBI-7371065,EBI-78260

GO - Molecular functioni

  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112025. 5 interactors.
IntActiP08922. 3 interactors.
MINTiMINT-2800684.
STRINGi9606.ENSP00000357494.

Chemistry databases

BindingDBiP08922.

Structurei

Secondary structure

12347
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1942 – 1944Combined sources3
Beta strandi1945 – 1952Combined sources8
Turni1955 – 1957Combined sources3
Beta strandi1959 – 1965Combined sources7
Turni1966 – 1968Combined sources3
Beta strandi1974 – 1981Combined sources8
Helixi1988 – 2002Combined sources15
Beta strandi2012 – 2016Combined sources5
Beta strandi2018 – 2021Combined sources4
Beta strandi2023 – 2027Combined sources5
Helixi2034 – 2043Combined sources10
Helixi2053 – 2072Combined sources20
Helixi2082 – 2084Combined sources3
Beta strandi2085 – 2088Combined sources4
Beta strandi2090 – 2094Combined sources5
Beta strandi2098 – 2100Combined sources3
Helixi2125 – 2127Combined sources3
Helixi2130 – 2135Combined sources6
Helixi2140 – 2155Combined sources16
Helixi2167 – 2175Combined sources9
Helixi2188 – 2197Combined sources10
Helixi2202 – 2204Combined sources3
Helixi2208 – 2227Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZBFX-ray2.20A1934-2232[»]
4UXLX-ray2.40A1934-2232[»]
ProteinModelPortaliP08922.
SMRiP08922.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini101 – 196Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST96
Domaini197 – 285Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST89
Domaini557 – 671Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST115
Domaini947 – 1042Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST96
Domaini1043 – 1150Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST108
Domaini1450 – 1556Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST107
Domaini1557 – 1656Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST100
Domaini1658 – 1751Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST94
Domaini1752 – 1854Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST103
Domaini1945 – 2222Protein kinasePROSITE-ProRule annotationAdd BLAST278

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

eggNOGiENOG410IQAA. Eukaryota.
ENOG410XSTC. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000137937.
HOVERGENiHBG058631.
InParanoidiP08922.
KOiK05088.
OMAiQQDALSF.
OrthoDBiEOG091G003T.
PhylomeDBiP08922.
TreeFamiTF351636.

Family and domain databases

CDDicd00063. FN3. 7 hits.
Gene3Di2.120.10.30. 3 hits.
2.60.40.10. 8 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR003961. FN3_dom.
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.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 9 hits.
SM00135. LY. 4 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.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNIYCLIPK LVNFATLGCL WISVVQCTVL NSCLKSCVTN LGQQLDLGTP
60 70 80 90 100
HNLSEPCIQG CHFWNSVDQK NCALKCRESC EVGCSSAEGA YEEEVLENAD
110 120 130 140 150
LPTAPFASSI GSHNMTLRWK SANFSGVKYI IQWKYAQLLG SWTYTKTVSR
160 170 180 190 200
PSYVVKPLHP FTEYIFRVVW IFTAQLQLYS PPSPSYRTHP HGVPETAPLI
210 220 230 240 250
RNIESSSPDT VEVSWDPPQF PGGPILGYNL RLISKNQKLD AGTQRTSFQF
260 270 280 290 300
YSTLPNTIYR FSIAAVNEVG EGPEAESSIT TSSSAVQQEE QWLFLSRKTS
310 320 330 340 350
LRKRSLKHLV DEAHCLRLDA IYHNITGISV DVHQQIVYFS EGTLIWAKKA
360 370 380 390 400
ANMSDVSDLR IFYRGSGLIS SISIDWLYQR MYFIMDELVC VCDLENCSNI
410 420 430 440 450
EEITPPSISA PQKIVADSYN GYVFYLLRDG IYRADLPVPS GRCAEAVRIV
460 470 480 490 500
ESCTLKDFAI KPQAKRIIYF NDTAQVFMST FLDGSASHLI LPRIPFADVK
510 520 530 540 550
SFACENNDFL VTDGKVIFQQ DALSFNEFIV GCDLSHIEEF GFGNLVIFGS
560 570 580 590 600
SSQLHPLPGR PQELSVLFGS HQALVQWKPP ALAIGANVIL ISDIIELFEL
610 620 630 640 650
GPSAWQNWTY EVKVSTQDPP EVTHIFLNIS GTMLNVPELQ SAMKYKVSVR
660 670 680 690 700
ASSPKRPGPW SEPSVGTTLV PASEPPFIMA VKEDGLWSKP LNSFGPGEFL
710 720 730 740 750
SSDIGNVSDM DWYNNSLYYS DTKGDVFVWL LNGTDISENY HLPSIAGAGA
760 770 780 790 800
LAFEWLGHFL YWAGKTYVIQ RQSVLTGHTD IVTHVKLLVN DMVVDSVGGY
810 820 830 840 850
LYWTTLYSVE STRLNGESSL VLQTQPWFSG KKVIALTLDL SDGLLYWLVQ
860 870 880 890 900
DSQCIHLYTA VLRGQSTGDT TITEFAAWST SEISQNALMY YSGRLFWING
910 920 930 940 950
FRIITTQEIG QKTSVSVLEP ARFNQFTIIQ TSLKPLPGNF SFTPKVIPDS
960 970 980 990 1000
VQESSFRIEG NASSFQILWN GPPAVDWGVV FYSVEFSAHS KFLASEQHSL
1010 1020 1030 1040 1050
PVFTVEGLEP YALFNLSVTP YTYWGKGPKT SLSLRAPETV PSAPENPRIF
1060 1070 1080 1090 1100
ILPSGKCCNK NEVVVEFRWN KPKHENGVLT KFEIFYNISN QSITNKTCED
1110 1120 1130 1140 1150
WIAVNVTPSV MSFQLEGMSP RCFIAFQVRA FTSKGPGPYA DVVKSTTSEI
1160 1170 1180 1190 1200
NPFPHLITLL GNKIVFLDMD QNQVVWTFSA ERVISAVCYT ADNEMGYYAE
1210 1220 1230 1240 1250
GDSLFLLHLH NRSSSELFQD SLVFDITVIT IDWISRHLYF ALKESQNGMQ
1260 1270 1280 1290 1300
VFDVDLEHKV KYPREVKIHN RNSTIISFSV YPLLSRLYWT EVSNFGYQMF
1310 1320 1330 1340 1350
YYSIISHTLH RILQPTATNQ QNKRNQCSCN VTEFELSGAM AIDTSNLEKP
1360 1370 1380 1390 1400
LIYFAKAQEI WAMDLEGCQC WRVITVPAML AGKTLVSLTV DGDLIYWIIT
1410 1420 1430 1440 1450
AKDSTQIYQA KKGNGAIVSQ VKALRSRHIL AYSSVMQPFP DKAFLSLASD
1460 1470 1480 1490 1500
TVEPTILNAT NTSLTIRLPL AKTNLTWYGI TSPTPTYLVY YAEVNDRKNS
1510 1520 1530 1540 1550
SDLKYRILEF QDSIALIEDL QPFSTYMIQI AVKNYYSDPL EHLPPGKEIW
1560 1570 1580 1590 1600
GKTKNGVPEA VQLINTTVRS DTSLIISWRE SHKPNGPKES VRYQLAISHL
1610 1620 1630 1640 1650
ALIPETPLRQ SEFPNGRLTL LVTRLSGGNI YVLKVLACHS EEMWCTESHP
1660 1670 1680 1690 1700
VTVEMFNTPE KPYSLVPENT SLQFNWKAPL NVNLIRFWVE LQKWKYNEFY
1710 1720 1730 1740 1750
HVKTSCSQGP AYVCNITNLQ PYTSYNVRVV VVYKTGENST SLPESFKTKA
1760 1770 1780 1790 1800
GVPNKPGIPK LLEGSKNSIQ WEKAEDNGCR ITYYILEIRK STSNNLQNQN
1810 1820 1830 1840 1850
LRWKMTFNGS CSSVCTWKSK NLKGIFQFRV VAANNLGFGE YSGISENIIL
1860 1870 1880 1890 1900
VGDDFWIPET SFILTIIVGI FLVVTIPLTF VWHRRLKNQK SAKEGVTVLI
1910 1920 1930 1940 1950
NEDKELAELR GLAAGVGLAN ACYAIHTLPT QEEIENLPAF PREKLTLRLL
1960 1970 1980 1990 2000
LGSGAFGEVY EGTAVDILGV GSGEIKVAVK TLKKGSTDQE KIEFLKEAHL
2010 2020 2030 2040 2050
MSKFNHPNIL KQLGVCLLNE PQYIILELME GGDLLTYLRK ARMATFYGPL
2060 2070 2080 2090 2100
LTLVDLVDLC VDISKGCVYL ERMHFIHRDL AARNCLVSVK DYTSPRIVKI
2110 2120 2130 2140 2150
GDFGLARDIY KNDYYRKRGE GLLPVRWMAP ESLMDGIFTT QSDVWSFGIL
2160 2170 2180 2190 2200
IWEILTLGHQ PYPAHSNLDV LNYVQTGGRL EPPRNCPDDL WNLMTQCWAQ
2210 2220 2230 2240 2250
EPDQRPTFHR IQDQLQLFRN FFLNSIYKSR DEANNSGVIN ESFEGEDGDV
2260 2270 2280 2290 2300
ICLNSDDIMP VALMETKNRE GLNYMVLATE CGQGEEKSEG PLGSQESESC
2310 2320 2330 2340
GLRKEEKEPH ADKDFCQEKQ VAYCPSGKPE GLNYACLTHS GYGDGSD
Length:2,347
Mass (Da):263,915
Last modified:February 20, 2007 - v3
Checksum:i98902B9A59ACB8F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2246 – 2260EDGDV…DDIMP → KFDSSEFSSFRCTVN in AAA60277 (PubMed:3023956).CuratedAdd BLAST15
Sequence conflicti2262A → V in AAA60278 (PubMed:2352949).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04144213N → S.1 PublicationCorresponds to variant rs45606237dbSNPEnsembl.1
Natural variantiVAR_041443126G → V.1 PublicationCorresponds to variant rs34245787dbSNPEnsembl.1
Natural variantiVAR_030648145T → P.1 PublicationCorresponds to variant rs1998206dbSNPEnsembl.1
Natural variantiVAR_030649167R → Q.1 PublicationCorresponds to variant rs2243380dbSNPEnsembl.1
Natural variantiVAR_041444224P → S.1 PublicationCorresponds to variant rs55959124dbSNPEnsembl.1
Natural variantiVAR_041445338Y → C.1 PublicationCorresponds to variant rs55707658dbSNPEnsembl.1
Natural variantiVAR_041446370S → P.1 PublicationCorresponds to variant rs56274823dbSNPEnsembl.1
Natural variantiVAR_041447419Y → H in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041448537I → M.1 PublicationCorresponds to variant rs28639589dbSNPEnsembl.1
Natural variantiVAR_041449653S → F.1 PublicationCorresponds to variant rs34203286dbSNPEnsembl.1
Natural variantiVAR_049712790N → S.Corresponds to variant rs34582164dbSNPEnsembl.1
Natural variantiVAR_041450865Q → H in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0306501109S → L.1 PublicationCorresponds to variant rs2229079dbSNPEnsembl.1
Natural variantiVAR_0414511239Y → F.1 PublicationCorresponds to variant rs56192249dbSNPEnsembl.1
Natural variantiVAR_0414521353Y → S.1 PublicationCorresponds to variant rs35269727dbSNPEnsembl.1
Natural variantiVAR_0414531370C → R.1 PublicationCorresponds to variant rs36106063dbSNPEnsembl.1
Natural variantiVAR_0306511439F → S.Corresponds to variant rs17079086dbSNPEnsembl.1
Natural variantiVAR_0414541506R → G.1 PublicationCorresponds to variant rs35841892dbSNPEnsembl.1
Natural variantiVAR_0306521776D → H.1 PublicationCorresponds to variant rs12664076dbSNPEnsembl.1
Natural variantiVAR_0306531902E → K.1 PublicationCorresponds to variant rs9489124dbSNPEnsembl.1
Natural variantiVAR_0414551999H → N.1 PublicationCorresponds to variant rs45569132dbSNPEnsembl.1
Natural variantiVAR_0414562003K → R in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0306542039R → H.Corresponds to variant rs3752566dbSNPEnsembl.1
Natural variantiVAR_0414572138F → S in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0414582203D → N.1 PublicationCorresponds to variant rs556427413dbSNPEnsembl.1
Natural variantiVAR_0414592213D → E.1 PublicationCorresponds to variant rs75510639dbSNPEnsembl.1
Natural variantiVAR_0306552213D → N.2 PublicationsCorresponds to variant rs529038dbSNPEnsembl.1
Natural variantiVAR_0414602228K → Q.2 PublicationsCorresponds to variant rs529156dbSNPEnsembl.1
Natural variantiVAR_0306562229S → C.2 PublicationsCorresponds to variant rs619203dbSNPEnsembl.1
Natural variantiVAR_0306572240N → K.1 PublicationCorresponds to variant rs210968dbSNPEnsembl.1
Natural variantiVAR_0497132328K → R.Corresponds to variant rs35932630dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34353 mRNA. Translation: AAA60278.1.
Z98880, AL132671 Genomic DNA. Translation: CAI42374.1.
AL132671, Z98880 Genomic DNA. Translation: CAI23378.1.
M13599
, M13368, M13591, M13592, M13593, M13594, M13595, M13596, M13597, M13598 Genomic DNA. Translation: AAA60277.1.
M13880 mRNA. Translation: AAA36580.1.
CCDSiCCDS5116.1.
PIRiA35512. TVHURS.
RefSeqiNP_002935.2. NM_002944.2.
UniGeneiHs.1041.

Genome annotation databases

EnsembliENST00000368508; ENSP00000357494; ENSG00000047936.
GeneIDi6098.
KEGGihsa:6098.
UCSCiuc003pxp.2. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34353 mRNA. Translation: AAA60278.1.
Z98880, AL132671 Genomic DNA. Translation: CAI42374.1.
AL132671, Z98880 Genomic DNA. Translation: CAI23378.1.
M13599
, M13368, M13591, M13592, M13593, M13594, M13595, M13596, M13597, M13598 Genomic DNA. Translation: AAA60277.1.
M13880 mRNA. Translation: AAA36580.1.
CCDSiCCDS5116.1.
PIRiA35512. TVHURS.
RefSeqiNP_002935.2. NM_002944.2.
UniGeneiHs.1041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZBFX-ray2.20A1934-2232[»]
4UXLX-ray2.40A1934-2232[»]
ProteinModelPortaliP08922.
SMRiP08922.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112025. 5 interactors.
IntActiP08922. 3 interactors.
MINTiMINT-2800684.
STRINGi9606.ENSP00000357494.

Chemistry databases

BindingDBiP08922.
ChEMBLiCHEMBL5568.
GuidetoPHARMACOLOGYi1840.

PTM databases

iPTMnetiP08922.
PhosphoSitePlusiP08922.

Polymorphism and mutation databases

BioMutaiROS1.
DMDMi126302596.

Proteomic databases

EPDiP08922.
PaxDbiP08922.
PeptideAtlasiP08922.
PRIDEiP08922.

Protocols and materials databases

DNASUi6098.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368508; ENSP00000357494; ENSG00000047936.
GeneIDi6098.
KEGGihsa:6098.
UCSCiuc003pxp.2. human.

Organism-specific databases

CTDi6098.
DisGeNETi6098.
GeneCardsiROS1.
H-InvDBHIX0207391.
HGNCiHGNC:10261. ROS1.
HPAiHPA049098.
MIMi165020. gene.
neXtProtiNX_P08922.
OpenTargetsiENSG00000047936.
PharmGKBiPA34633.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQAA. Eukaryota.
ENOG410XSTC. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000137937.
HOVERGENiHBG058631.
InParanoidiP08922.
KOiK05088.
OMAiQQDALSF.
OrthoDBiEOG091G003T.
PhylomeDBiP08922.
TreeFamiTF351636.

Enzyme and pathway databases

BioCyciZFISH:HS00597-MONOMER.
BRENDAi2.7.10.1. 2681.
SignaLinkiP08922.
SIGNORiP08922.

Miscellaneous databases

ChiTaRSiROS1. human.
GeneWikiiROS1_(gene).
GenomeRNAii6098.
PROiP08922.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000047936.
CleanExiHS_ROS1.
ExpressionAtlasiP08922. baseline and differential.
GenevisibleiP08922. HS.

Family and domain databases

CDDicd00063. FN3. 7 hits.
Gene3Di2.120.10.30. 3 hits.
2.60.40.10. 8 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR003961. FN3_dom.
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.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 9 hits.
SM00135. LY. 4 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.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiROS1_HUMAN
AccessioniPrimary (citable) accession number: P08922
Secondary accession number(s): Q15368, Q5TDB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 20, 2007
Last modified: November 30, 2016
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.