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Q04912

- RON_HUMAN

UniProt

Q04912 - RON_HUMAN

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Protein

Macrophage-stimulating protein receptor

Gene

MST1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1114 – 11141ATP
Active sitei1208 – 12081Proton acceptor1 Publication
Binding sitei1212 – 12121ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1088 – 10969ATP
Nucleotide bindingi1161 – 11644ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. macrophage colony-stimulating factor receptor activity Source: ProtInc

GO - Biological processi

  1. cellular component movement Source: ProtInc
  2. defense response Source: ProtInc
  3. innate immune response Source: UniProtKB-KW
  4. macrophage colony-stimulating factor signaling pathway Source: GOC
  5. multicellular organismal development Source: InterPro
  6. positive regulation of cell proliferation Source: ProtInc
  7. positive regulation of MAP kinase activity Source: UniProtKB
  8. positive regulation of protein kinase B signaling Source: UniProtKB
  9. response to virus Source: UniProtKB
  10. signal transduction Source: ProtInc
  11. single fertilization Source: ProtInc
  12. transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiQ04912.

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage-stimulating protein receptor (EC:2.7.10.1)
Short name:
MSP receptor
Alternative name(s):
CDw136
Protein-tyrosine kinase 8
p185-Ron
CD_antigen: CD136
Cleaved into the following 2 chains:
Gene namesi
Name:MST1R
Synonyms:PTK8, RON
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7381. MST1R.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. integral component of plasma membrane Source: ProtInc
  3. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 14001376Macrophage-stimulating protein receptorPRO_0000024452Add
BLAST
Chaini25 – 304280Macrophage-stimulating protein receptor alpha chainSequence AnalysisPRO_0000024453Add
BLAST
Chaini310 – 14001091Macrophage-stimulating protein receptor beta chainSequence AnalysisPRO_0000024454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi101 ↔ 1041 PublicationPROSITE-ProRule annotation
Disulfide bondi107 ↔ 1621 PublicationPROSITE-ProRule annotation
Disulfide bondi135 ↔ 1431 PublicationPROSITE-ProRule annotation
Disulfide bondi174 ↔ 1771 PublicationPROSITE-ProRule annotation
Disulfide bondi300 ↔ 3671 PublicationPROSITE-ProRule annotation
Disulfide bondi385 ↔ 4071 PublicationPROSITE-ProRule annotation
Disulfide bondi386 ↔ 4221 PublicationPROSITE-ProRule annotation
Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi488 – 4881N-linked (GlcNAc...)1 Publication
Disulfide bondi527 ↔ 5451 PublicationPROSITE-ProRule annotation
Disulfide bondi533 ↔ 5671 PublicationPROSITE-ProRule annotation
Disulfide bondi536 ↔ 5521 PublicationPROSITE-ProRule annotation
Disulfide bondi548 ↔ 5581 PublicationPROSITE-ProRule annotation
Glycosylationi654 – 6541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi841 – 8411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi897 – 8971N-linked (GlcNAc...)Sequence Analysis
Modified residuei1238 – 12381Phosphotyrosine; by autocatalysis2 Publications
Modified residuei1239 – 12391Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1353 – 13531Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1360 – 13601Phosphotyrosine; by autocatalysis1 Publication

Post-translational modificationi

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.2 Publications
Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ04912.
PaxDbiQ04912.
PRIDEiQ04912.

PTM databases

PhosphoSiteiQ04912.

Expressioni

Tissue specificityi

Expressed in colon, skin, lung and bone marrow.1 Publication

Gene expression databases

BgeeiQ04912.
CleanExiHS_MST1R.
ExpressionAtlasiQ04912. baseline and differential.
GenevestigatoriQ04912.

Organism-specific databases

HPAiCAB008972.
HPA007657.
HPA008180.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PLXNB1O431573EBI-2637518,EBI-1111488
PLXNB2O150312EBI-2637518,EBI-722004
PLXNB3Q9ULL42EBI-2637518,EBI-311073

Protein-protein interaction databases

BioGridi110592. 19 interactions.
DIPiDIP-6029N.
IntActiQ04912. 9 interactions.
MINTiMINT-6539690.
STRINGi9606.ENSP00000296474.

Structurei

Secondary structure

1
1400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 453
Beta strandi48 – 503
Beta strandi55 – 628
Beta strandi68 – 747
Beta strandi77 – 815
Beta strandi87 – 926
Helixi102 – 1054
Beta strandi108 – 1103
Beta strandi120 – 1267
Turni127 – 1304
Beta strandi131 – 1388
Helixi139 – 1413
Beta strandi143 – 1519
Beta strandi154 – 1574
Beta strandi184 – 1918
Beta strandi194 – 2018
Helixi205 – 2084
Beta strandi209 – 2113
Beta strandi215 – 2217
Beta strandi233 – 2353
Helixi239 – 2424
Beta strandi248 – 2558
Beta strandi258 – 26811
Beta strandi275 – 28814
Beta strandi294 – 3029
Beta strandi316 – 3183
Beta strandi320 – 3289
Helixi331 – 3377
Beta strandi344 – 3518
Beta strandi365 – 3706
Helixi371 – 38616
Beta strandi387 – 3893
Turni399 – 4013
Helixi422 – 4243
Beta strandi433 – 4364
Turni438 – 4458
Beta strandi448 – 4569
Beta strandi459 – 4668
Beta strandi469 – 4757
Beta strandi485 – 4917
Beta strandi503 – 5053
Beta strandi508 – 5136
Beta strandi516 – 5216
Helixi527 – 5293
Helixi533 – 5386
Helixi541 – 5433
Beta strandi549 – 5535
Helixi555 – 5573
Turni559 – 5613
Helixi1064 – 10696
Helixi1071 – 10733
Helixi1077 – 10793
Beta strandi1080 – 109112
Beta strandi1094 – 11029
Beta strandi1104 – 11063
Beta strandi1108 – 11169
Helixi1122 – 113615
Beta strandi1148 – 11503
Beta strandi1153 – 11553
Beta strandi1158 – 11614
Helixi1169 – 11746
Helixi1182 – 120120
Helixi1211 – 12133
Beta strandi1214 – 12163
Beta strandi1222 – 12243
Turni1232 – 12354
Helixi1236 – 12394
Helixi1250 – 12534
Helixi1256 – 12594
Helixi1266 – 128217
Turni1287 – 12904
Helixi1293 – 12953
Helixi1296 – 13016
Helixi1314 – 132310
Helixi1328 – 13303
Helixi1334 – 134714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PLSX-ray2.24A1060-1357[»]
4FWWX-ray1.85A42-568[»]
4QT8X-ray3.00A/B25-683[»]
ProteinModelPortaliQ04912.
SMRiQ04912. Positions 42-769, 1060-1377.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 957933ExtracellularSequence AnalysisAdd
BLAST
Topological domaini979 – 1400422CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei958 – 97821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 522492SemaPROSITE-ProRule annotationAdd
BLAST
Domaini569 – 671103IPT/TIG 1Add
BLAST
Domaini684 – 76784IPT/TIG 2Add
BLAST
Domaini770 – 86091IPT/TIG 3Add
BLAST
Domaini1082 – 1345264Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi306 – 3094Poly-Arg
Compositional biasi962 – 9687Poly-Leu

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
Contains 3 IPT/TIG domains.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 Sema domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000220900.
HOVERGENiHBG104342.
InParanoidiQ04912.
KOiK05100.
OMAiHFGVVYH.
OrthoDBiEOG7J70DR.
PhylomeDBiQ04912.
TreeFamiTF317402.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProiIPR013783. 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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 2 hits.
[Graphical view]
PIRSFiPIRSF000617. TyrPK_HGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00429. IPT. 3 hits.
SM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF81296. SSF81296. 3 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS51004. SEMA. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform RON (identifier: Q04912-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MELLPPLPQS FLLLLLLPAK PAAGEDWQCP RTPYAASRDF DVKYVVPSFS
60 70 80 90 100
AGGLVQAMVT YEGDRNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG
110 120 130 140 150
CQTCAACGPG PHGPPGDTDT KVLVLDPALP ALVSCGSSLQ GRCFLHDLEP
160 170 180 190 200
QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS PLGTRVTVVE QGQASYFYVA
210 220 230 240 250
SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK HLVSYSIEYV
260 270 280 290 300
HSFHTGAFVY FLTVQPASVT DDPSALHTRL ARLSATEPEL GDYRELVLDC
310 320 330 340 350
RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF
360 370 380 390 400
VTGKDGGPGV GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF
410 420 430 440 450
FQSPSFCPNP PGLEALSPNT SCRHFPLLVS SSFSRVDLFN GLLGPVQVTA
460 470 480 490 500
LYVTRLDNVT VAHMGTMDGR ILQVELVRSL NYLLYVSNFS LGDSGQPVQR
510 520 530 540 550
DVSRLGDHLL FASGDQVFQV PIQGPGCRHF LTCGRCLRAW HFMGCGWCGN
560 570 580 590 600
MCGQQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG
610 620 630 640 650
LVPEGTHQVT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV
660 670 680 690 700
GPTNVSLTVT NMPPGKHFRV DGTSVLRGFS FMEPVLIAVQ PLFGPRAGGT
710 720 730 740 750
CLTLEGQSLS VGTSRAVLVN GTECLLARVS EGQLLCATPP GATVASVPLS
760 770 780 790 800
LQVGGAQVPG SWTFQYREDP VVLSISPNCG YINSHITICG QHLTSAWHLV
810 820 830 840 850
LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VRDPQGWVAG NLSARGDGAA
860 870 880 890 900
GFTLPGFRFL PPPHPPSANL VPLKPEEHAI KFEYIGLGAV ADCVGINVTV
910 920 930 940 950
GGESCQHEFR GDMVVCPLPP SLQLGQDGAP LQVCVDGECH ILGRVVRPGP
960 970 980 990 1000
DGVPQSTLLG ILLPLLLLVA ALATALVFSY WWRRKQLVLP PNLNDLASLD
1010 1020 1030 1040 1050
QTAGATPLPI LYSGSDYRSG LALPAIDGLD STTCVHGASF SDSEDESCVP
1060 1070 1080 1090 1100
LLRKESIQLR DLDSALLAEV KDVLIPHERV VTHSDRVIGK GHFGVVYHGE
1110 1120 1130 1140 1150
YIDQAQNRIQ CAIKSLSRIT EMQQVEAFLR EGLLMRGLNH PNVLALIGIM
1160 1170 1180 1190 1200
LPPEGLPHVL LPYMCHGDLL QFIRSPQRNP TVKDLISFGL QVARSMEYLA
1210 1220 1230 1240 1250
EQKFVHRDLA ARNCMLDESF TVKVADFGLA RDILDREYYS VQQHRHARLP
1260 1270 1280 1290 1300
VKWMALESLQ TYRFTTKSDV WSFGVLLWEL LTRGAPPYRH IDPFDLTHFL
1310 1320 1330 1340 1350
AQGRRLPQPE YCPDSLYQVM QQCWEADPAV RPTFRVLVGE VEQIVSALLG
1360 1370 1380 1390 1400
DHYVQLPATY MNLGPSTSHE MNVRPEQPQF SPMPGNVRRP RPLSEPPRPT
Length:1,400
Mass (Da):152,271
Last modified:April 20, 2010 - v2
Checksum:iEB5CA79ABC69A882
GO
Isoform Delta-RON (identifier: Q04912-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,351
Mass (Da):147,277
Checksum:i23ACE5B9330EEA0B
GO
Isoform RON-1 (identifier: Q04912-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     475-495: ELVRSLNYLLYVSNFSLGDSG → GPHPHSPLALGPCLHPHFAHI
     496-1400: Missing.

Show »
Length:495
Mass (Da):52,519
Checksum:i3F99D0A454B25721
GO
Isoform RON-2 (identifier: Q04912-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     411-516: Missing.
     628-647: PVPRKDFVEEFECELEPLGT → YNLVPPLPFPEGGNQAAPSP
     648-1400: Missing.

Show »
Length:541
Mass (Da):57,721
Checksum:i9BC028F4170B1BFC
GO
Isoform RON-3 (identifier: Q04912-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     884-907: YIGLGAVADCVGINVTVGGESCQH → VSVRDRGRDSWGSESRGQPTGWSS
     908-1400: Missing.

Show »
Length:907
Mass (Da):97,315
Checksum:iDDC3A5776146ECCB
GO
Isoform RON-4 (identifier: Q04912-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:647
Mass (Da):69,265
Checksum:iBE4234918FE98C33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091A → G in CAA49634. (PubMed:8386824)Curated
Sequence conflicti813 – 8131R → RQ in ACF47620. (PubMed:18593464)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751R → S.1 Publication
Corresponds to variant rs35887539 [ dbSNP | Ensembl ].
VAR_041768
Natural varianti95 – 951P → T.1 Publication
Corresponds to variant rs55908300 [ dbSNP | Ensembl ].
VAR_041769
Natural varianti185 – 1851R → C.1 Publication
Corresponds to variant rs55633379 [ dbSNP | Ensembl ].
VAR_041770
Natural varianti322 – 3221R → Q.2 Publications
Corresponds to variant rs2230593 [ dbSNP | Ensembl ].
VAR_006350
Natural varianti356 – 3561G → D.1 Publication
Corresponds to variant rs35924402 [ dbSNP | Ensembl ].
VAR_041771
Natural varianti434 – 4341S → L.1 Publication
Corresponds to variant rs2230591 [ dbSNP | Ensembl ].
VAR_029238
Natural varianti440 – 4401N → S.
Corresponds to variant rs2230592 [ dbSNP | Ensembl ].
VAR_029239
Natural varianti465 – 4651G → D.1 Publication
Corresponds to variant rs34564898 [ dbSNP | Ensembl ].
VAR_041772
Natural varianti504 – 5041R → C.1 Publication
Corresponds to variant rs34350470 [ dbSNP | Ensembl ].
VAR_041773
Natural varianti523 – 5231Q → R.2 Publications
Corresponds to variant rs2230590 [ dbSNP | Ensembl ].
VAR_041774
Natural varianti613 – 6131Q → P.1 Publication
Corresponds to variant rs35986685 [ dbSNP | Ensembl ].
VAR_041775
Natural varianti900 – 9001V → M.1 Publication
Corresponds to variant rs56091918 [ dbSNP | Ensembl ].
VAR_041776
Natural varianti1195 – 11951S → G.1 Publication
Corresponds to variant rs7433231 [ dbSNP | Ensembl ].
VAR_061749
Natural varianti1304 – 13041R → G.1 Publication
VAR_041777
Natural varianti1335 – 13351R → G.1 Publication
Corresponds to variant rs1062633 [ dbSNP | Ensembl ].
VAR_024577
Natural varianti1360 – 13601Y → C.1 Publication
Corresponds to variant rs56330223 [ dbSNP | Ensembl ].
VAR_041778

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei411 – 516106Missing in isoform RON-2. 1 PublicationVSP_038919Add
BLAST
Alternative sequencei475 – 49521ELVRS…LGDSG → GPHPHSPLALGPCLHPHFAH I in isoform RON-1. 1 PublicationVSP_038920Add
BLAST
Alternative sequencei496 – 1400905Missing in isoform RON-1. 1 PublicationVSP_038921Add
BLAST
Alternative sequencei628 – 64720PVPRK…EPLGT → YNLVPPLPFPEGGNQAAPSP in isoform RON-2 and isoform RON-4. 1 PublicationVSP_038922Add
BLAST
Alternative sequencei648 – 1400753Missing in isoform RON-2 and isoform RON-4. 1 PublicationVSP_038923Add
BLAST
Alternative sequencei884 – 93249Missing in isoform Delta-RON. CuratedVSP_005007Add
BLAST
Alternative sequencei884 – 90724YIGLG…ESCQH → VSVRDRGRDSWGSESRGQPT GWSS in isoform RON-3. 1 PublicationVSP_038924Add
BLAST
Alternative sequencei908 – 1400493Missing in isoform RON-3. 1 PublicationVSP_038925Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2807.1. [Q04912-1]
CCDS58833.1. [Q04912-2]
PIRiI38185.
RefSeqiNP_001231866.1. NM_001244937.1.
NP_002438.2. NM_002447.2.
UniGeneiHs.517973.

Genome annotation databases

EnsembliENST00000296474; ENSP00000296474; ENSG00000164078.
ENST00000344206; ENSP00000341325; ENSG00000164078.
GeneIDi4486.
KEGGihsa:4486.
UCSCiuc003cxy.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]

Polymorphism databases

DMDMi294862462.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS2807.1. [Q04912-1 ]
CCDS58833.1. [Q04912-2 ]
PIRi I38185.
RefSeqi NP_001231866.1. NM_001244937.1.
NP_002438.2. NM_002447.2.
UniGenei Hs.517973.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3PLS X-ray 2.24 A 1060-1357 [» ]
4FWW X-ray 1.85 A 42-568 [» ]
4QT8 X-ray 3.00 A/B 25-683 [» ]
ProteinModelPortali Q04912.
SMRi Q04912. Positions 42-769, 1060-1377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110592. 19 interactions.
DIPi DIP-6029N.
IntActi Q04912. 9 interactions.
MINTi MINT-6539690.
STRINGi 9606.ENSP00000296474.

Chemistry

BindingDBi Q04912.
ChEMBLi CHEMBL2689.
GuidetoPHARMACOLOGYi 1816.

PTM databases

PhosphoSitei Q04912.

Polymorphism databases

DMDMi 294862462.

Proteomic databases

MaxQBi Q04912.
PaxDbi Q04912.
PRIDEi Q04912.

Protocols and materials databases

DNASUi 4486.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296474 ; ENSP00000296474 ; ENSG00000164078 .
ENST00000344206 ; ENSP00000341325 ; ENSG00000164078 .
GeneIDi 4486.
KEGGi hsa:4486.
UCSCi uc003cxy.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

CTDi 4486.
GeneCardsi GC03M049924.
HGNCi HGNC:7381. MST1R.
HPAi CAB008972.
HPA007657.
HPA008180.
MIMi 600168. gene.
neXtProti NX_Q04912.
PharmGKBi PA31186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000220900.
HOVERGENi HBG104342.
InParanoidi Q04912.
KOi K05100.
OMAi HFGVVYH.
OrthoDBi EOG7J70DR.
PhylomeDBi Q04912.
TreeFami TF317402.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki Q04912.

Miscellaneous databases

ChiTaRSi MST1R. human.
GeneWikii MST1R.
GenomeRNAii 4486.
NextBioi 17355.
PROi Q04912.
SOURCEi Search...

Gene expression databases

Bgeei Q04912.
CleanExi HS_MST1R.
ExpressionAtlasi Q04912. baseline and differential.
Genevestigatori Q04912.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProi IPR013783. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 2 hits.
[Graphical view ]
PIRSFi PIRSF000617. TyrPK_HGF-R. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00429. IPT. 3 hits.
SM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF81296. SSF81296. 3 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS51004. SEMA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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: PHOSPHORYLATION AT TYR-1238; TYR-1239; TYR-1353 AND TYR-1360, 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. 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.
    , 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.

Entry informationi

Entry nameiRON_HUMAN
AccessioniPrimary (citable) accession number: Q04912
Secondary accession number(s): B5A944
, B5A945, B5A946, B5A947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 20, 2010
Last modified: October 29, 2014
This is version 159 of the entry and version 2 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3