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Q04912 (RON_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage-stimulating protein receptor

Short name=MSP receptor
EC=2.7.10.1
Alternative name(s):
CDw136
Protein-tyrosine kinase 8
p185-Ron
CD_antigen=CD136
Gene names
Name:MST1R
Synonyms:PTK8, RON
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Plays also a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. Ref.7 Ref.8 Ref.16

Catalytic activity

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

Enzyme regulation

In its inactive state, the C-terminal tail interacts with the catalytic domain and inhibits the kinase activity. Upon ligand binding, the C-terminal tail is displaced and becomes phosphorylated, thus increasing the kinase activity. Ref.15

Subunit structure

Heterodimer of an alpha chain and a beta chain which are disulfide linked. Binds PLXNB1. Associates with and is negatively regulated by HYAL2. Interacts when phosphorylated with downstream effectors including PIK3R1, PCLG1, GRB2 and GAB1. Interacts with integrin beta1/ITGB1 in a ligand-independent fashion. Ref.5 Ref.9 Ref.10 Ref.13 Ref.14 Ref.18

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in colon, skin, lung and bone marrow. Ref.6

Post-translational modification

Proteolytic processing yields the two subunits.

Autophosphorylated in response to ligand binding on Tyr-1238 and Tyr-1239 in the kinase domain leading to further phosphorylation of Tyr-1353 and Tyr-1360 in the C-terminal multifunctional docking site. Ref.15 Ref.19

Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 3 IPT/TIG domains.

Contains 1 protein kinase domain.

Contains 1 Sema domain.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular component movement

Traceable author statement PubMed 9045873. Source: ProtInc

defense response

Traceable author statement PubMed 9045873. Source: ProtInc

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

macrophage colony-stimulating factor signaling pathway

Traceable author statement PubMed 9045873. Source: GOC

multicellular organismal development

Inferred from electronic annotation. Source: InterPro

positive regulation of MAP kinase activity

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement PubMed 10871856. Source: ProtInc

positive regulation of protein kinase B signaling

Inferred from direct assay Ref.13. Source: UniProtKB

response to virus

Inferred from direct assay Ref.13. Source: UniProtKB

signal transduction

Traceable author statement Ref.7. Source: ProtInc

single fertilization

Traceable author statement PubMed 9045873. Source: ProtInc

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.7. Source: ProtInc

stress fiber

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction Ref.13. Source: UniProtKB

macrophage colony-stimulating factor receptor activity

Traceable author statement PubMed 9045873. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform RON (identifier: Q04912-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Delta-RON (identifier: Q04912-2)

The sequence of this isoform differs from the canonical sequence as follows:
     884-932: Missing.
Note: Lacks part of the extracellular domain, oligomerizes and is constitutively activated.
Isoform RON-1 (identifier: Q04912-3)

The sequence of this isoform differs from the canonical sequence as follows:
     475-495: ELVRSLNYLLYVSNFSLGDSG → GPHPHSPLALGPCLHPHFAHI
     496-1400: Missing.
Isoform RON-2 (identifier: Q04912-4)

The sequence of this isoform differs from the canonical sequence as follows:
     411-516: Missing.
     628-647: PVPRKDFVEEFECELEPLGT → YNLVPPLPFPEGGNQAAPSP
     648-1400: Missing.
Isoform RON-3 (identifier: Q04912-5)

The sequence of this isoform differs from the canonical sequence as follows:
     884-907: YIGLGAVADCVGINVTVGGESCQH → VSVRDRGRDSWGSESRGQPTGWSS
     908-1400: Missing.
Isoform RON-4 (identifier: Q04912-6)

The sequence of this isoform differs from the canonical sequence as follows:
     628-647: PVPRKDFVEEFECELEPLGT → YNLVPPLPFPEGGNQAAPSP
     648-1400: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 14001376Macrophage-stimulating protein receptor
PRO_0000024452
Chain25 – 304280Macrophage-stimulating protein receptor alpha chain Potential
PRO_0000024453
Chain310 – 14001091Macrophage-stimulating protein receptor beta chain Potential
PRO_0000024454

Regions

Topological domain25 – 957933Extracellular Potential
Transmembrane958 – 97821Helical; Potential
Topological domain979 – 1400422Cytoplasmic Potential
Domain31 – 522492Sema
Domain569 – 671103IPT/TIG 1
Domain684 – 76784IPT/TIG 2
Domain770 – 86091IPT/TIG 3
Domain1082 – 1345264Protein kinase
Nucleotide binding1088 – 10969ATP
Nucleotide binding1161 – 11644ATP
Compositional bias306 – 3094Poly-Arg
Compositional bias962 – 9687Poly-Leu

Sites

Active site12081Proton acceptor Probable
Binding site11141ATP
Binding site12121ATP

Amino acid modifications

Modified residue12381Phosphotyrosine; by autocatalysis Probable
Modified residue12391Phosphotyrosine; by autocatalysis Probable
Modified residue13531Phosphotyrosine; by autocatalysis
Modified residue13601Phosphotyrosine; by autocatalysis
Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Ref.20
Glycosylation6541N-linked (GlcNAc...) Potential
Glycosylation7201N-linked (GlcNAc...) Potential
Glycosylation8411N-linked (GlcNAc...) Potential
Glycosylation8971N-linked (GlcNAc...) Potential
Disulfide bond101 ↔ 104 Ref.20
Disulfide bond107 ↔ 162 Ref.20
Disulfide bond135 ↔ 143 Ref.20
Disulfide bond174 ↔ 177 Ref.20
Disulfide bond300 ↔ 367 Ref.20
Disulfide bond385 ↔ 407 Ref.20
Disulfide bond386 ↔ 422 Ref.20
Disulfide bond527 ↔ 545 Ref.20
Disulfide bond533 ↔ 567 Ref.20
Disulfide bond536 ↔ 552 Ref.20
Disulfide bond548 ↔ 558 Ref.20

Natural variations

Alternative sequence411 – 516106Missing in isoform RON-2.
VSP_038919
Alternative sequence475 – 49521ELVRS…LGDSG → GPHPHSPLALGPCLHPHFAH I in isoform RON-1.
VSP_038920
Alternative sequence496 – 1400905Missing in isoform RON-1.
VSP_038921
Alternative sequence628 – 64720PVPRK…EPLGT → YNLVPPLPFPEGGNQAAPSP in isoform RON-2 and isoform RON-4.
VSP_038922
Alternative sequence648 – 1400753Missing in isoform RON-2 and isoform RON-4.
VSP_038923
Alternative sequence884 – 93249Missing in isoform Delta-RON.
VSP_005007
Alternative sequence884 – 90724YIGLG…ESCQH → VSVRDRGRDSWGSESRGQPT GWSS in isoform RON-3.
VSP_038924
Alternative sequence908 – 1400493Missing in isoform RON-3.
VSP_038925
Natural variant751R → S. Ref.21
Corresponds to variant rs35887539 [ dbSNP | Ensembl ].
VAR_041768
Natural variant951P → T. Ref.21
Corresponds to variant rs55908300 [ dbSNP | Ensembl ].
VAR_041769
Natural variant1851R → C. Ref.21
Corresponds to variant rs55633379 [ dbSNP | Ensembl ].
VAR_041770
Natural variant3221R → Q. Ref.1 Ref.21
Corresponds to variant rs2230593 [ dbSNP | Ensembl ].
VAR_006350
Natural variant3561G → D. Ref.21
Corresponds to variant rs35924402 [ dbSNP | Ensembl ].
VAR_041771
Natural variant4341S → L. Ref.21
Corresponds to variant rs2230591 [ dbSNP | Ensembl ].
VAR_029238
Natural variant4401N → S.
Corresponds to variant rs2230592 [ dbSNP | Ensembl ].
VAR_029239
Natural variant4651G → D. Ref.21
Corresponds to variant rs34564898 [ dbSNP | Ensembl ].
VAR_041772
Natural variant5041R → C. Ref.21
Corresponds to variant rs34350470 [ dbSNP | Ensembl ].
VAR_041773
Natural variant5231Q → R. Ref.1 Ref.21
Corresponds to variant rs2230590 [ dbSNP | Ensembl ].
VAR_041774
Natural variant6131Q → P. Ref.21
Corresponds to variant rs35986685 [ dbSNP | Ensembl ].
VAR_041775
Natural variant9001V → M. Ref.21
Corresponds to variant rs56091918 [ dbSNP | Ensembl ].
VAR_041776
Natural variant11951S → G. Ref.1
Corresponds to variant rs7433231 [ dbSNP | Ensembl ].
VAR_061749
Natural variant13041R → G. Ref.21
VAR_041777
Natural variant13351R → G. Ref.21
Corresponds to variant rs1062633 [ dbSNP | Ensembl ].
VAR_024577
Natural variant13601Y → C. Ref.21
Corresponds to variant rs56330223 [ dbSNP | Ensembl ].
VAR_041778

Experimental info

Sequence conflict2091A → G in CAA49634. Ref.1
Sequence conflict8131R → RQ in ACF47620. Ref.3

Secondary structure

............................................................................................................................................... 1400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform RON [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: EB5CA79ABC69A882

FASTA1,400152,271
        10         20         30         40         50         60 
MELLPPLPQS FLLLLLLPAK PAAGEDWQCP RTPYAASRDF DVKYVVPSFS AGGLVQAMVT 

        70         80         90        100        110        120 
YEGDRNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPPGDTDT 

       130        140        150        160        170        180 
KVLVLDPALP ALVSCGSSLQ GRCFLHDLEP QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS 

       190        200        210        220        230        240 
PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK 

       250        260        270        280        290        300 
HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DDPSALHTRL ARLSATEPEL GDYRELVLDC 

       310        320        330        340        350        360 
RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VTGKDGGPGV 

       370        380        390        400        410        420 
GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEALSPNT 

       430        440        450        460        470        480 
SCRHFPLLVS SSFSRVDLFN GLLGPVQVTA LYVTRLDNVT VAHMGTMDGR ILQVELVRSL 

       490        500        510        520        530        540 
NYLLYVSNFS LGDSGQPVQR DVSRLGDHLL FASGDQVFQV PIQGPGCRHF LTCGRCLRAW 

       550        560        570        580        590        600 
HFMGCGWCGN MCGQQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG 

       610        620        630        640        650        660 
LVPEGTHQVT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV GPTNVSLTVT 

       670        680        690        700        710        720 
NMPPGKHFRV DGTSVLRGFS FMEPVLIAVQ PLFGPRAGGT CLTLEGQSLS VGTSRAVLVN 

       730        740        750        760        770        780 
GTECLLARVS EGQLLCATPP GATVASVPLS LQVGGAQVPG SWTFQYREDP VVLSISPNCG 

       790        800        810        820        830        840 
YINSHITICG QHLTSAWHLV LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VRDPQGWVAG 

       850        860        870        880        890        900 
NLSARGDGAA GFTLPGFRFL PPPHPPSANL VPLKPEEHAI KFEYIGLGAV ADCVGINVTV 

       910        920        930        940        950        960 
GGESCQHEFR GDMVVCPLPP SLQLGQDGAP LQVCVDGECH ILGRVVRPGP DGVPQSTLLG 

       970        980        990       1000       1010       1020 
ILLPLLLLVA ALATALVFSY WWRRKQLVLP PNLNDLASLD QTAGATPLPI LYSGSDYRSG 

      1030       1040       1050       1060       1070       1080 
LALPAIDGLD STTCVHGASF SDSEDESCVP LLRKESIQLR DLDSALLAEV KDVLIPHERV 

      1090       1100       1110       1120       1130       1140 
VTHSDRVIGK GHFGVVYHGE YIDQAQNRIQ CAIKSLSRIT EMQQVEAFLR EGLLMRGLNH 

      1150       1160       1170       1180       1190       1200 
PNVLALIGIM LPPEGLPHVL LPYMCHGDLL QFIRSPQRNP TVKDLISFGL QVARSMEYLA 

      1210       1220       1230       1240       1250       1260 
EQKFVHRDLA ARNCMLDESF TVKVADFGLA RDILDREYYS VQQHRHARLP VKWMALESLQ 

      1270       1280       1290       1300       1310       1320 
TYRFTTKSDV WSFGVLLWEL LTRGAPPYRH IDPFDLTHFL AQGRRLPQPE YCPDSLYQVM 

      1330       1340       1350       1360       1370       1380 
QQCWEADPAV RPTFRVLVGE VEQIVSALLG DHYVQLPATY MNLGPSTSHE MNVRPEQPQF 

      1390       1400 
SPMPGNVRRP RPLSEPPRPT 

« Hide

Isoform Delta-RON [UniParc].

Checksum: 23ACE5B9330EEA0B
Show »

FASTA1,351147,277
Isoform RON-1 [UniParc].

Checksum: 3F99D0A454B25721
Show »

FASTA49552,519
Isoform RON-2 [UniParc].

Checksum: 9BC028F4170B1BFC
Show »

FASTA54157,721
Isoform RON-3 [UniParc].

Checksum: DDC3A5776146ECCB
Show »

FASTA90797,315
Isoform RON-4 [UniParc].

Checksum: BE4234918FE98C33
Show »

FASTA64769,265

References

« Hide 'large scale' references
[1]"A novel putative receptor protein tyrosine kinase of the met family."
Ronsin C., Muscatelli F., Mattei M.-G., Breathnach R.
Oncogene 8:1195-1202(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RON), VARIANTS GLN-322; ARG-523 AND GLY-1195.
Tissue: Keratinocyte.
[2]"A splicing variant of the RON transcript induces constitutive tyrosine kinase activity and an invasive phenotype."
Collesi C., Santoro M.M., Gaudino G., Comoglio P.M.
Mol. Cell. Biol. 16:5518-5526(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[3]"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RON-1; RON-2; RON-3 AND RON-4).
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"A novel recognition motif for phosphatidylinositol 3-kinase binding mediates its association with the hepatocyte growth factor/scatter factor receptor."
Ponzetto C., Bardelli A., Maina F., Longati P., Panayotou G., Dhand R., Waterfield M.D., Comoglio P.M.
Mol. Cell. Biol. 13:4600-4608(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3R1.
[6]"RON is a heterodimeric tyrosine kinase receptor activated by the HGF homologue MSP."
Gaudino G., Follenzi A., Naldini L., Collesi C., Santoro M., Gallo K.A., Godowski P.J., Comoglio P.M.
EMBO J. 13:3524-3532(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Identification of the ron gene product as the receptor for the human macrophage stimulating protein."
Wang M.-H., Ronsin C., Gesnel M.-C., Coupey L., Skeel A., Leonard E.J., Breatnach R.
Science 266:117-119(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Proteolytic cleavage and activation of pro-macrophage-stimulating protein and upregulation of its receptor in tissue injury."
Nanney L.B., Skeel A., Luan J., Polis S., Richmond A., Wang M.H., Leonard E.J.
J. Invest. Dermatol. 111:573-581(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN WOUND HEALING RESPONSE.
[9]"Macrophage stimulating protein-induced epithelial cell adhesion is mediated by a PI3-K-dependent, but FAK-independent mechanism."
Danilkovitch A., Skeel A., Leonard E.J.
Exp. Cell Res. 248:575-582(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1.
[10]"Interaction of macrophage-stimulating protein with its receptor. Residues critical for beta chain binding and evidence for independent alpha chain binding."
Danilkovitch A., Miller M., Leonard E.J.
J. Biol. Chem. 274:29937-29943(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MST1.
[11]"Macrophage-stimulating protein and RON receptor tyrosine kinase: potential regulators of macrophage inflammatory activities."
Wang M.H., Zhou Y.Q., Chen Y.Q.
Scand. J. Immunol. 56:545-553(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[12]"c-Cbl is a critical modulator of the Ron tyrosine kinase receptor."
Penengo L., Rubin C., Yarden Y., Gaudino G.
Oncogene 22:3669-3679(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[13]"Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and mediates transformation of epithelial cells by jaagsiekte sheep retrovirus."
Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D., Liu S.-L., Miller A.D., Lerman M.I.
Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HYAL2.
[14]"Interplay between scatter factor receptors and B plexins controls invasive growth."
Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.
Oncogene 23:5131-5137(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1.
[15]"The C terminus of RON tyrosine kinase plays an autoinhibitory role."
Yokoyama N., Ischenko I., Hayman M.J., Miller W.T.
J. Biol. Chem. 280:8893-8900(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, ENZYME REGULATION.
[16]"The RON receptor tyrosine kinase promotes MSP-independent cell spreading and survival in breast epithelial cells."
Feres K.J., Ischenko I., Hayman M.J.
Oncogene 28:279-288(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Distinct involvement of the Gab1 and Grb2 adaptor proteins in signal transduction by the related receptor tyrosine kinases RON and MET."
Chaudhuri A., Xie M.H., Yang B., Mahapatra K., Liu J., Marsters S., Bodepudi S., Ashkenazi A.
J. Biol. Chem. 286:32762-32774(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAB1 AND GRB2.
[19]"The crystal structure of a constitutively active mutant RON kinase suggests an intramolecular autophosphorylation hypothesis."
Wang J., Steinbacher S., Augustin M., Schreiner P., Epstein D., Mulvihill M.J., Crew A.P.
Biochemistry 49:7972-7974(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1060-1357 IN COMPLEX WITH AMP-PNP AND MAGNESIUM, ACTIVE SITE, PHOSPHORYLATION AT TYR-1238.
[20]"Crystal structure of the Sema-PSI extracellular domain of human RON receptor tyrosine kinase."
Chao K.L., Tsai I.W., Chen C., Herzberg O.
PLoS ONE 7:E41912-E41912(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 42-568, GLYCOSYLATION AT ASN-488, DISULFIDE BONDS.
[21]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-75; THR-95; CYS-185; GLN-322; ASP-356; LEU-434; ASP-465; CYS-504; ARG-523; PRO-613; MET-900; GLY-1304; GLY-1335 AND CYS-1360.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70040 mRNA. Translation: CAA49634.1.
EU826582 mRNA. Translation: ACF47618.1.
EU826583 mRNA. Translation: ACF47619.1.
EU826584 mRNA. Translation: ACF47620.1.
EU826585 mRNA. Translation: ACF47621.1.
AC105935 Genomic DNA. No translation available.
PIRI38185.
RefSeqNP_001231866.1. NM_001244937.1.
NP_002438.2. NM_002447.2.
UniGeneHs.517973.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PLSX-ray2.24A1060-1357[»]
4FWWX-ray1.85A42-568[»]
ProteinModelPortalQ04912.
SMRQ04912. Positions 42-769, 1060-1377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110592. 19 interactions.
DIPDIP-6029N.
IntActQ04912. 8 interactions.
MINTMINT-6539690.
STRING9606.ENSP00000296474.

Chemistry

BindingDBQ04912.
ChEMBLCHEMBL2689.
GuidetoPHARMACOLOGY1816.

PTM databases

PhosphoSiteQ04912.

Polymorphism databases

DMDM294862462.

Proteomic databases

PaxDbQ04912.
PRIDEQ04912.

Protocols and materials databases

DNASU4486.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296474; ENSP00000296474; ENSG00000164078. [Q04912-1]
ENST00000344206; ENSP00000341325; ENSG00000164078. [Q04912-2]
GeneID4486.
KEGGhsa:4486.
UCSCuc003cxy.4. human. [Q04912-1]
uc011bdc.2. human. [Q04912-2]
uc011bdd.2. human. [Q04912-5]
uc011bde.1. human. [Q04912-6]
uc011bdf.1. human. [Q04912-4]
uc011bdg.2. human. [Q04912-3]

Organism-specific databases

CTD4486.
GeneCardsGC03M049924.
HGNCHGNC:7381. MST1R.
HPACAB008972.
HPA007657.
HPA008180.
MIM600168. gene.
neXtProtNX_Q04912.
PharmGKBPA31186.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000220900.
HOVERGENHBG104342.
InParanoidQ04912.
KOK05100.
OMAHFGVVYH.
OrthoDBEOG7J70DR.
PhylomeDBQ04912.
TreeFamTF317402.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkQ04912.

Gene expression databases

ArrayExpressQ04912.
BgeeQ04912.
CleanExHS_MST1R.
GenevestigatorQ04912.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR011009. Kinase-like_dom.
IPR016201. Plexin-like_fold.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001627. Semap_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016244. Tyr_kinase_HGF/MSP_rcpt.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 2 hits.
[Graphical view]
PIRSFPIRSF000617. TyrPK_HGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00429. IPT. 3 hits.
SM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF81296. SSF81296. 3 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMST1R. human.
GeneWikiMST1R.
GenomeRNAi4486.
NextBio17355.
PROQ04912.
SOURCESearch...

Entry information

Entry nameRON_HUMAN
AccessionPrimary (citable) accession number: Q04912
Secondary accession number(s): B5A944 expand/collapse secondary AC list , B5A945, B5A946, B5A947
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries