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Database: UniProt
Entry: P08922
LinkDB: P08922
Original site: P08922 
ID   ROS1_HUMAN              Reviewed;        2347 AA.
AC   P08922; Q15368; Q5TDB5;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 3.
DT   29-OCT-2014, entry version 155.
DE   RecName: Full=Proto-oncogene tyrosine-protein kinase ROS;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene c-Ros;
DE   AltName: Full=Proto-oncogene c-Ros-1;
DE   AltName: Full=Receptor tyrosine kinase c-ros oncogene 1;
DE   AltName: Full=c-Ros receptor tyrosine kinase;
DE   Flags: Precursor;
GN   Name=ROS1; Synonyms=MCF3, ROS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-2213; GLN-2228 AND
RP   CYS-2229.
RX   PubMed=2352949; DOI=10.1073/pnas.87.12.4799;
RA   Birchmeier C., O'Neill K., Riggs M., Wigler M.;
RT   "Characterization of ROS1 cDNA from a human glioblastoma cell line.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4799-4803(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1790-2260.
RX   PubMed=3023956;
RA   Matsushime H., Wang L.-H., Shibuya M.;
RT   "Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma
RT   virus encodes for a transmembrane receptorlike molecule.";
RL   Mol. Cell. Biol. 6:3000-3004(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1854-2347.
RX   PubMed=3785223;
RA   Birchmeier C., Birnbaum D., Waitches G., Fasano O., Wigler M.;
RT   "Characterization of an activated human ros gene.";
RL   Mol. Cell. Biol. 6:3109-3116(1986).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=8143271; DOI=10.1016/0165-4608(94)90128-7;
RA   Watkins D., Dion F., Poisson M., Delattre J.Y., Rouleau G.A.;
RT   "Analysis of oncogene expression in primary human gliomas: evidence
RT   for increased expression of the ros oncogene.";
RL   Cancer Genet. Cytogenet. 72:130-136(1994).
RN   [6]
RP   FUNCTION IN VAV3 ACTIVATION, AND INTERACTION WITH VAV3.
RX   PubMed=11094073; DOI=10.1128/MCB.20.24.9212-9224.2000;
RA   Zeng L., Sachdev P., Yan L., Chan J.L., Trenkle T., McClelland M.,
RA   Welsh J., Wang L.H.;
RT   "Vav3 mediates receptor protein tyrosine kinase signaling, regulates
RT   GTPase activity, modulates cell morphology, and induces cell
RT   transformation.";
RL   Mol. Cell. Biol. 20:9212-9224(2000).
RN   [7]
RP   DISEASE, CHROMOSOMAL TRANSLOCATION WITH GOPC, AND MUTAGENESIS OF
RP   LYS-1980.
RX   PubMed=12661006; DOI=10.1002/gcc.10207;
RA   Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H.,
RA   Housman D.;
RT   "Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma
RT   with an interstitial del(6)(q21q21).";
RL   Genes Chromosomes Cancer 37:58-71(2003).
RN   [8]
RP   PHOSPHORYLATION AT TYR-2274 AND TYR-2334, AND MUTAGENESIS OF TYR-2274
RP   AND TYR-2334.
RX   PubMed=12538861; DOI=10.1073/pnas.242741799;
RA   Charest A., Kheifets V., Park J., Lane K., McMahon K., Nutt C.L.,
RA   Housman D.;
RT   "Oncogenic targeting of an activated tyrosine kinase to the Golgi
RT   apparatus in a glioblastoma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:916-921(2003).
RN   [9]
RP   FUNCTION IN CELL PROLIFERATION AND DIFFERENTATION, FUNCTION IN
RP   PHOSPHORYLATION OF PTPN11, AND INTERACTION WITH PTPN11.
RX   PubMed=16885344; DOI=10.1158/0008-5472.CAN-06-1193;
RA   Charest A., Wilker E.W., McLaughlin M.E., Lane K., Gowda R., Coven S.,
RA   McMahon K., Kovach S., Feng Y., Yaffe M.B., Jacks T., Housman D.;
RT   "ROS fusion tyrosine kinase activates a SH2 domain-containing
RT   phosphatase-2/phosphatidylinositol 3-kinase/mammalian target of
RT   rapamycin signaling axis to form glioblastoma in mice.";
RL   Cancer Res. 66:7473-7481(2006).
RN   [10]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-13; VAL-126; PRO-145; GLN-167;
RP   SER-224; CYS-338; PRO-370; HIS-419; MET-537; PHE-653; HIS-865;
RP   LEU-1109; PHE-1239; SER-1353; ARG-1370; GLY-1506; HIS-1776; LYS-1902;
RP   ASN-1999; ARG-2003; SER-2138; ASN-2203; GLU-2213; ASN-2213; GLN-2228;
RP   CYS-2229 AND LYS-2240.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Orphan receptor tyrosine kinase (RTK) that plays a role
CC       in epithelial cell differentiation and regionalization of the
CC       proximal epididymal epithelium. May activate several downstream
CC       signaling pathways related to cell differentiation, proliferation,
CC       growth and survival including the PI3 kinase-mTOR signaling
CC       pathway. Mediates the phosphorylation of PTPN11, an activator of
CC       this pathway. May also phosphorylate and activate the
CC       transcription factor STAT3 to control anchorage-independent cell
CC       growth. Mediates the phosphorylation and the activation of VAV3, a
CC       guanine nucleotide exchange factor regulating cell morphology. May
CC       activate other downstream signaling proteins including AKT1,
CC       MAPK1, MAPK3, IRS1 and PLCG2. {ECO:0000269|PubMed:11094073,
CC       ECO:0000269|PubMed:16885344}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028}.
CC   -!- ENZYME REGULATION: Inhibited by dephosphorylation by PTPN6.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PTPN6 (via SH2 1 domain); the interaction
CC       is direct and promotes ROS1 dephosphorylation (By similarity).
CC       Interacts with PTPN11; may activate the PI3 kinase-mTOR signaling
CC       pathway. Interacts with VAV3; constitutive interaction mediating
CC       VAV3 phosphorylation. {ECO:0000250, ECO:0000269|PubMed:11094073,
CC       ECO:0000269|PubMed:16885344}.
CC   -!- INTERACTION:
CC       P18031:PTPN1; NbExp=3; IntAct=EBI-7371065, EBI-968788;
CC       P29350:PTPN6; NbExp=2; IntAct=EBI-7371065, EBI-78260;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Expression is increased in
CC       primary gliomas. {ECO:0000269|PubMed:8143271}.
CC   -!- PTM: Phosphorylated. Probably autophosphorylates. Phosphorylation
CC       at Tyr-2274 is required for the interaction with PTPN6 that
CC       mediates ROS1 dephosphorylation (By similarity). Phosphorylation
CC       at Tyr-2274 stimulates the kinase activity and the activation of
CC       the ERK1 signaling cascade (By similarity). Phosphorylation at
CC       Tyr-2274 and/or Tyr-2334 recruits PTPN11. {ECO:0000250,
CC       ECO:0000269|PubMed:12538861}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ROS1 is found in
CC       a glioblastoma multiforme sample. An intra-chromosomal deletion
CC       del(6)(q21q21) is responsible for the formation of GOPC-ROS1
CC       chimeric protein which is localized to the Golgi and has a
CC       constitutive receptor tyrosine kinase activity. A SLC34A2-ROS1
CC       chimeric protein produced in non-small cell lung cancer cells also
CC       retains a constitutive kinase activity. A third type of chimeric
CC       protein CD74-ROS1 was also identified in those cells.
CC       {ECO:0000269|PubMed:12661006}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 9 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; M34353; AAA60278.1; -; mRNA.
DR   EMBL; Z98880; CAI42374.1; -; Genomic_DNA.
DR   EMBL; AL132671; CAI42374.1; JOINED; Genomic_DNA.
DR   EMBL; AL132671; CAI23378.1; -; Genomic_DNA.
DR   EMBL; Z98880; CAI23378.1; JOINED; Genomic_DNA.
DR   EMBL; M13599; AAA60277.1; -; Genomic_DNA.
DR   EMBL; M13368; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13591; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13592; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13593; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13594; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13595; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13596; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13597; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13598; AAA60277.1; JOINED; Genomic_DNA.
DR   EMBL; M13880; AAA36580.1; -; mRNA.
DR   CCDS; CCDS5116.1; -.
DR   PIR; A35512; TVHURS.
DR   RefSeq; NP_002935.2; NM_002944.2.
DR   UniGene; Hs.1041; -.
DR   PDB; 3ZBF; X-ray; 2.20 A; A=1934-2232.
DR   PDBsum; 3ZBF; -.
DR   ProteinModelPortal; P08922; -.
DR   SMR; P08922; 192-276, 632-668, 943-1147, 1484-1537, 1711-1849, 1881-2229.
DR   BioGrid; 112025; 5.
DR   IntAct; P08922; 3.
DR   MINT; MINT-2800684; -.
DR   STRING; 9606.ENSP00000357494; -.
DR   BindingDB; P08922; -.
DR   ChEMBL; CHEMBL5568; -.
DR   GuidetoPHARMACOLOGY; 1840; -.
DR   PhosphoSite; P08922; -.
DR   DMDM; 126302596; -.
DR   PaxDb; P08922; -.
DR   PRIDE; P08922; -.
DR   DNASU; 6098; -.
DR   Ensembl; ENST00000368508; ENSP00000357494; ENSG00000047936.
DR   GeneID; 6098; -.
DR   KEGG; hsa:6098; -.
DR   UCSC; uc003pxp.1; human.
DR   CTD; 6098; -.
DR   GeneCards; GC06M117609; -.
DR   H-InvDB; HIX0207391; -.
DR   HGNC; HGNC:10261; ROS1.
DR   HPA; HPA049098; -.
DR   MIM; 165020; gene.
DR   neXtProt; NX_P08922; -.
DR   PharmGKB; PA34633; -.
DR   eggNOG; COG0515; -.
DR   GeneTree; ENSGT00760000118818; -.
DR   HOGENOM; HOG000137937; -.
DR   HOVERGEN; HBG058631; -.
DR   InParanoid; P08922; -.
DR   KO; K05088; -.
DR   OMA; YWLVQDS; -.
DR   OrthoDB; EOG7GN2KT; -.
DR   PhylomeDB; P08922; -.
DR   TreeFam; TF351636; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   SignaLink; P08922; -.
DR   ChiTaRS; ROS1; human.
DR   GeneWiki; ROS1_(gene); -.
DR   GenomeRNAi; 6098; -.
DR   NextBio; 23723; -.
DR   PRO; PR:P08922; -.
DR   Bgee; P08922; -.
DR   CleanEx; HS_ROS1; -.
DR   ExpressionAtlas; P08922; baseline and differential.
DR   Genevestigator; P08922; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR   GO; GO:0016049; P:cell growth; IDA:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   GO; GO:0002066; P:columnar/cuboidal epithelial cell development; ISS:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:GOC.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0010966; P:regulation of phosphate transport; IEA:Ensembl.
DR   GO; GO:0032006; P:regulation of TOR signaling; IDA:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   Gene3D; 2.120.10.30; -; 3.
DR   Gene3D; 2.60.40.10; -; 7.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 9.
DR   SMART; SM00135; LY; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; SSF49265; 5.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50853; FN3; 9.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell membrane; Chromosomal rearrangement;
KW   Complete proteome; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Proto-oncogene; Receptor;
KW   Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   2347       Proto-oncogene tyrosine-protein kinase
FT                                ROS.
FT                                /FTId=PRO_0000016722.
FT   TOPO_DOM     28   1859       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1860   1882       Helical. {ECO:0000255}.
FT   TOPO_DOM   1883   2347       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      101    196       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      197    285       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      557    671       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      947   1042       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1043   1150       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1450   1556       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1557   1656       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1658   1751       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1752   1854       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1945   2222       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND    1951   1959       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE   2079   2079       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING    1980   1980       ATP. {ECO:0000305}.
FT   SITE       1852   1853       Breakpoint for translocation to form
FT                                SLC34A2-ROS1 and CD74-ROS1 fusion
FT                                proteins.
FT   SITE       1880   1881       Breakpoint for translocation to form
FT                                GOPC-ROS1 fusion protein.
FT   MOD_RES    2274   2274       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000305|PubMed:12538861}.
FT   MOD_RES    2334   2334       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000305|PubMed:12538861}.
FT   CARBOHYD     52     52       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    114    114       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    324    324       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    352    352       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    396    396       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    471    471       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    607    607       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    628    628       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    706    706       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    714    714       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    732    732       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    939    939       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    961    961       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1015   1015       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1087   1087       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1090   1090       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1095   1095       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1211   1211       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1272   1272       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1330   1330       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1458   1458       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1461   1461       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1474   1474       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1499   1499       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1565   1565       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1669   1669       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1715   1715       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1738   1738       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1808   1808       N-linked (GlcNAc...). {ECO:0000255}.
FT   VARIANT      13     13       N -> S (in dbSNP:rs45606237).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041442.
FT   VARIANT     126    126       G -> V (in dbSNP:rs34245787).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041443.
FT   VARIANT     145    145       T -> P (in dbSNP:rs1998206).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_030648.
FT   VARIANT     167    167       R -> Q (in dbSNP:rs2243380).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_030649.
FT   VARIANT     224    224       P -> S (in dbSNP:rs55959124).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041444.
FT   VARIANT     338    338       Y -> C (in dbSNP:rs55707658).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041445.
FT   VARIANT     370    370       S -> P (in dbSNP:rs56274823).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041446.
FT   VARIANT     419    419       Y -> H (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041447.
FT   VARIANT     537    537       I -> M (in dbSNP:rs28639589).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041448.
FT   VARIANT     653    653       S -> F (in dbSNP:rs34203286).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041449.
FT   VARIANT     790    790       N -> S (in dbSNP:rs34582164).
FT                                /FTId=VAR_049712.
FT   VARIANT     865    865       Q -> H (in a lung large cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041450.
FT   VARIANT    1109   1109       S -> L (in dbSNP:rs2229079).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_030650.
FT   VARIANT    1239   1239       Y -> F (in dbSNP:rs56192249).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041451.
FT   VARIANT    1353   1353       Y -> S (in dbSNP:rs35269727).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041452.
FT   VARIANT    1370   1370       C -> R (in dbSNP:rs36106063).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041453.
FT   VARIANT    1439   1439       F -> S (in dbSNP:rs17079086).
FT                                /FTId=VAR_030651.
FT   VARIANT    1506   1506       R -> G (in dbSNP:rs35841892).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041454.
FT   VARIANT    1776   1776       D -> H (in dbSNP:rs12664076).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_030652.
FT   VARIANT    1902   1902       E -> K (in dbSNP:rs9489124).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_030653.
FT   VARIANT    1999   1999       H -> N (in dbSNP:rs45569132).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041455.
FT   VARIANT    2003   2003       K -> R (in a colorectal adenocarcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041456.
FT   VARIANT    2039   2039       R -> H (in dbSNP:rs3752566).
FT                                /FTId=VAR_030654.
FT   VARIANT    2138   2138       F -> S (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041457.
FT   VARIANT    2203   2203       D -> N. {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041458.
FT   VARIANT    2213   2213       D -> E (in dbSNP:rs75510639).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041459.
FT   VARIANT    2213   2213       D -> N (in dbSNP:rs529038).
FT                                {ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:2352949}.
FT                                /FTId=VAR_030655.
FT   VARIANT    2228   2228       K -> Q (in dbSNP:rs529156).
FT                                {ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:2352949}.
FT                                /FTId=VAR_041460.
FT   VARIANT    2229   2229       S -> C (in dbSNP:rs619203).
FT                                {ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:2352949}.
FT                                /FTId=VAR_030656.
FT   VARIANT    2240   2240       N -> K (in dbSNP:rs210968).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_030657.
FT   VARIANT    2328   2328       K -> R (in dbSNP:rs35932630).
FT                                /FTId=VAR_049713.
FT   MUTAGEN    1980   1980       K->M: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:12661006}.
FT   MUTAGEN    2274   2274       Y->F: Loss of phosphorylation at Y-2274
FT                                and loss of interaction with PTPN11.
FT                                {ECO:0000269|PubMed:12538861}.
FT   MUTAGEN    2334   2334       Y->F: Loss of phosphorylation at Y-2334
FT                                and loss of interaction with PTPN11.
FT                                {ECO:0000269|PubMed:12538861}.
FT   CONFLICT   2246   2260       EDGDVICLNSDDIMP -> KFDSSEFSSFRCTVN (in
FT                                Ref. 3; AAA60277). {ECO:0000305}.
FT   CONFLICT   2262   2262       A -> V (in Ref. 1; AAA60278).
FT                                {ECO:0000305}.
FT   HELIX      1942   1944
FT   STRAND     1945   1952
FT   STRAND     1959   1965
FT   STRAND     1974   1981
FT   HELIX      1988   2002
FT   STRAND     2012   2016
FT   STRAND     2018   2021
FT   STRAND     2023   2027
FT   HELIX      2034   2043
FT   HELIX      2053   2072
FT   HELIX      2082   2084
FT   STRAND     2085   2088
FT   STRAND     2090   2094
FT   STRAND     2098   2100
FT   HELIX      2125   2127
FT   HELIX      2130   2135
FT   HELIX      2140   2155
FT   HELIX      2167   2175
FT   HELIX      2188   2197
FT   HELIX      2202   2204
FT   HELIX      2208   2227
SQ   SEQUENCE   2347 AA;  263915 MW;  98902B9A59ACB8F5 CRC64;
     MKNIYCLIPK LVNFATLGCL WISVVQCTVL NSCLKSCVTN LGQQLDLGTP HNLSEPCIQG
     CHFWNSVDQK NCALKCRESC EVGCSSAEGA YEEEVLENAD LPTAPFASSI GSHNMTLRWK
     SANFSGVKYI IQWKYAQLLG SWTYTKTVSR PSYVVKPLHP FTEYIFRVVW IFTAQLQLYS
     PPSPSYRTHP HGVPETAPLI RNIESSSPDT VEVSWDPPQF PGGPILGYNL RLISKNQKLD
     AGTQRTSFQF YSTLPNTIYR FSIAAVNEVG EGPEAESSIT TSSSAVQQEE QWLFLSRKTS
     LRKRSLKHLV DEAHCLRLDA IYHNITGISV DVHQQIVYFS EGTLIWAKKA ANMSDVSDLR
     IFYRGSGLIS SISIDWLYQR MYFIMDELVC VCDLENCSNI EEITPPSISA PQKIVADSYN
     GYVFYLLRDG IYRADLPVPS GRCAEAVRIV ESCTLKDFAI KPQAKRIIYF NDTAQVFMST
     FLDGSASHLI LPRIPFADVK SFACENNDFL VTDGKVIFQQ DALSFNEFIV GCDLSHIEEF
     GFGNLVIFGS SSQLHPLPGR PQELSVLFGS HQALVQWKPP ALAIGANVIL ISDIIELFEL
     GPSAWQNWTY EVKVSTQDPP EVTHIFLNIS GTMLNVPELQ SAMKYKVSVR ASSPKRPGPW
     SEPSVGTTLV PASEPPFIMA VKEDGLWSKP LNSFGPGEFL SSDIGNVSDM DWYNNSLYYS
     DTKGDVFVWL LNGTDISENY HLPSIAGAGA LAFEWLGHFL YWAGKTYVIQ RQSVLTGHTD
     IVTHVKLLVN DMVVDSVGGY LYWTTLYSVE STRLNGESSL VLQTQPWFSG KKVIALTLDL
     SDGLLYWLVQ DSQCIHLYTA VLRGQSTGDT TITEFAAWST SEISQNALMY YSGRLFWING
     FRIITTQEIG QKTSVSVLEP ARFNQFTIIQ TSLKPLPGNF SFTPKVIPDS VQESSFRIEG
     NASSFQILWN GPPAVDWGVV FYSVEFSAHS KFLASEQHSL PVFTVEGLEP YALFNLSVTP
     YTYWGKGPKT SLSLRAPETV PSAPENPRIF ILPSGKCCNK NEVVVEFRWN KPKHENGVLT
     KFEIFYNISN QSITNKTCED WIAVNVTPSV MSFQLEGMSP RCFIAFQVRA FTSKGPGPYA
     DVVKSTTSEI NPFPHLITLL GNKIVFLDMD QNQVVWTFSA ERVISAVCYT ADNEMGYYAE
     GDSLFLLHLH NRSSSELFQD SLVFDITVIT IDWISRHLYF ALKESQNGMQ VFDVDLEHKV
     KYPREVKIHN RNSTIISFSV YPLLSRLYWT EVSNFGYQMF YYSIISHTLH RILQPTATNQ
     QNKRNQCSCN VTEFELSGAM AIDTSNLEKP LIYFAKAQEI WAMDLEGCQC WRVITVPAML
     AGKTLVSLTV DGDLIYWIIT AKDSTQIYQA KKGNGAIVSQ VKALRSRHIL AYSSVMQPFP
     DKAFLSLASD TVEPTILNAT NTSLTIRLPL AKTNLTWYGI TSPTPTYLVY YAEVNDRKNS
     SDLKYRILEF QDSIALIEDL QPFSTYMIQI AVKNYYSDPL EHLPPGKEIW GKTKNGVPEA
     VQLINTTVRS DTSLIISWRE SHKPNGPKES VRYQLAISHL ALIPETPLRQ SEFPNGRLTL
     LVTRLSGGNI YVLKVLACHS EEMWCTESHP VTVEMFNTPE KPYSLVPENT SLQFNWKAPL
     NVNLIRFWVE LQKWKYNEFY HVKTSCSQGP AYVCNITNLQ PYTSYNVRVV VVYKTGENST
     SLPESFKTKA GVPNKPGIPK LLEGSKNSIQ WEKAEDNGCR ITYYILEIRK STSNNLQNQN
     LRWKMTFNGS CSSVCTWKSK NLKGIFQFRV VAANNLGFGE YSGISENIIL VGDDFWIPET
     SFILTIIVGI FLVVTIPLTF VWHRRLKNQK SAKEGVTVLI NEDKELAELR GLAAGVGLAN
     ACYAIHTLPT QEEIENLPAF PREKLTLRLL LGSGAFGEVY EGTAVDILGV GSGEIKVAVK
     TLKKGSTDQE KIEFLKEAHL MSKFNHPNIL KQLGVCLLNE PQYIILELME GGDLLTYLRK
     ARMATFYGPL LTLVDLVDLC VDISKGCVYL ERMHFIHRDL AARNCLVSVK DYTSPRIVKI
     GDFGLARDIY KNDYYRKRGE GLLPVRWMAP ESLMDGIFTT QSDVWSFGIL IWEILTLGHQ
     PYPAHSNLDV LNYVQTGGRL EPPRNCPDDL WNLMTQCWAQ EPDQRPTFHR IQDQLQLFRN
     FFLNSIYKSR DEANNSGVIN ESFEGEDGDV ICLNSDDIMP VALMETKNRE GLNYMVLATE
     CGQGEEKSEG PLGSQESESC GLRKEEKEPH ADKDFCQEKQ VAYCPSGKPE GLNYACLTHS
     GYGDGSD
//
DBGET integrated database retrieval system