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Protein

Macrophage-stimulating protein receptor

Gene

MST1R

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei1114ATP1
Active sitei1208Proton acceptor1 Publication1
Binding sitei1212ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1088 – 1096ATP9
Nucleotide bindingi1161 – 1164ATP4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • macrophage colony-stimulating factor receptor activity Source: ProtInc

GO - Biological processi

  • defense response Source: ProtInc
  • hepatocyte growth factor receptor signaling pathway Source: Reactome
  • innate immune response Source: UniProtKB-KW
  • movement of cell or subcellular component Source: ProtInc
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • response to virus Source: UniProtKB
  • signal transduction Source: ProtInc
  • single fertilization Source: ProtInc
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

BioCyciZFISH:HS09003-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-8852405. Signaling by MST1.
SignaLinkiQ04912.
SIGNORiQ04912.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:7381. MST1R.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 957ExtracellularSequence analysisAdd BLAST933
Transmembranei958 – 978HelicalSequence analysisAdd BLAST21
Topological domaini979 – 1400CytoplasmicSequence analysisAdd BLAST422

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
  • stress fiber Source: Ensembl
  • vacuole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Nasopharyngeal carcinoma, 3 (NPCA3)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of nasopharyngeal carcinoma, a malignant neoplasm that originates in the nasopharyngeal epithelium and includes 4 subtypes: keratinizing squamous cell, non-keratinizing, basaloid squamous cell, and papillary adenocarcinoma.
See also OMIM:617075
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076928306R → H in NPCA3. 1 Publication1
Natural variantiVAR_076929327A → T in NPCA3; unknown pathological significance. 1 Publication1
Natural variantiVAR_076930670V → G in NPCA3; unknown pathological significance. 1 Publication1
Natural variantiVAR_076931973A → T in NPCA3; unknown pathological significance. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4486.
MIMi255995. phenotype.
617075. phenotype.
PharmGKBiPA31186.

Chemistry databases

ChEMBLiCHEMBL2689.
GuidetoPHARMACOLOGYi1816.

Polymorphism and mutation databases

BioMutaiMST1R.
DMDMi294862462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000002445225 – 1400Macrophage-stimulating protein receptorAdd BLAST1376
ChainiPRO_000002445325 – 304Macrophage-stimulating protein receptor alpha chainSequence analysisAdd BLAST280
ChainiPRO_0000024454310 – 1400Macrophage-stimulating protein receptor beta chainSequence analysisAdd BLAST1091

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi66N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi101 ↔ 104PROSITE-ProRule annotation1 Publication
Disulfide bondi107 ↔ 162PROSITE-ProRule annotation1 Publication
Disulfide bondi135 ↔ 143PROSITE-ProRule annotation1 Publication
Disulfide bondi174 ↔ 177PROSITE-ProRule annotation1 Publication
Disulfide bondi300 ↔ 367PROSITE-ProRule annotation1 Publication
Disulfide bondi385 ↔ 407PROSITE-ProRule annotation1 Publication
Disulfide bondi386 ↔ 422PROSITE-ProRule annotation1 Publication
Glycosylationi419N-linked (GlcNAc...)Sequence analysis1
Glycosylationi458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi488N-linked (GlcNAc...)1 Publication1
Disulfide bondi527 ↔ 545PROSITE-ProRule annotation1 Publication
Disulfide bondi533 ↔ 567PROSITE-ProRule annotation1 Publication
Disulfide bondi536 ↔ 552PROSITE-ProRule annotation1 Publication
Disulfide bondi548 ↔ 558PROSITE-ProRule annotation1 Publication
Glycosylationi654N-linked (GlcNAc...)Sequence analysis1
Glycosylationi720N-linked (GlcNAc...)Sequence analysis1
Glycosylationi841N-linked (GlcNAc...)Sequence analysis1
Glycosylationi897N-linked (GlcNAc...)Sequence analysis1
Modified residuei1238Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1239Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1353Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1360Phosphotyrosine; by autocatalysis1 Publication1

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.
PeptideAtlasiQ04912.
PRIDEiQ04912.

PTM databases

iPTMnetiQ04912.
PhosphoSitePlusiQ04912.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000164078.
CleanExiHS_MST1R.
ExpressionAtlasiQ04912. baseline and differential.
GenevisibleiQ04912. HS.

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
MST1P269275EBI-2637518,EBI-6929133
PLXNB1O431573EBI-2637518,EBI-1111488
PLXNB2O150312EBI-2637518,EBI-722004
PLXNB3Q9ULL42EBI-2637518,EBI-311073

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110592. 23 interactors.
DIPiDIP-6029N.
IntActiQ04912. 15 interactors.
MINTiMINT-6539690.
STRINGi9606.ENSP00000296474.

Chemistry databases

BindingDBiQ04912.

Structurei

Secondary structure

11400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 45Combined sources3
Beta strandi48 – 50Combined sources3
Beta strandi55 – 62Combined sources8
Beta strandi64 – 66Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi77 – 81Combined sources5
Beta strandi87 – 92Combined sources6
Beta strandi96 – 98Combined sources3
Helixi102 – 105Combined sources4
Beta strandi108 – 110Combined sources3
Beta strandi120 – 126Combined sources7
Turni127 – 130Combined sources4
Beta strandi131 – 138Combined sources8
Helixi139 – 141Combined sources3
Beta strandi143 – 151Combined sources9
Beta strandi154 – 157Combined sources4
Beta strandi161 – 163Combined sources3
Turni166 – 168Combined sources3
Beta strandi184 – 191Combined sources8
Beta strandi194 – 201Combined sources8
Helixi205 – 208Combined sources4
Beta strandi209 – 211Combined sources3
Beta strandi215 – 221Combined sources7
Beta strandi233 – 235Combined sources3
Helixi239 – 242Combined sources4
Beta strandi248 – 255Combined sources8
Beta strandi258 – 268Combined sources11
Beta strandi269 – 271Combined sources3
Beta strandi275 – 288Combined sources14
Helixi290 – 292Combined sources3
Beta strandi294 – 302Combined sources9
Beta strandi309 – 311Combined sources3
Beta strandi316 – 318Combined sources3
Beta strandi320 – 328Combined sources9
Helixi331 – 337Combined sources7
Beta strandi344 – 351Combined sources8
Beta strandi365 – 370Combined sources6
Helixi371 – 386Combined sources16
Beta strandi387 – 389Combined sources3
Turni399 – 401Combined sources3
Beta strandi407 – 409Combined sources3
Helixi422 – 424Combined sources3
Beta strandi433 – 436Combined sources4
Turni438 – 445Combined sources8
Beta strandi448 – 456Combined sources9
Beta strandi459 – 466Combined sources8
Beta strandi469 – 475Combined sources7
Beta strandi485 – 491Combined sources7
Beta strandi503 – 505Combined sources3
Beta strandi508 – 513Combined sources6
Beta strandi516 – 521Combined sources6
Helixi527 – 529Combined sources3
Helixi533 – 538Combined sources6
Helixi541 – 543Combined sources3
Beta strandi549 – 553Combined sources5
Helixi555 – 557Combined sources3
Turni559 – 561Combined sources3
Beta strandi563 – 567Combined sources5
Beta strandi570 – 575Combined sources6
Beta strandi578 – 580Combined sources3
Beta strandi589 – 593Combined sources5
Beta strandi609 – 615Combined sources7
Beta strandi639 – 641Combined sources3
Beta strandi653 – 659Combined sources7
Beta strandi672 – 682Combined sources11
Helixi1064 – 1069Combined sources6
Helixi1071 – 1073Combined sources3
Helixi1077 – 1079Combined sources3
Beta strandi1080 – 1091Combined sources12
Beta strandi1094 – 1102Combined sources9
Beta strandi1104 – 1106Combined sources3
Beta strandi1108 – 1116Combined sources9
Helixi1122 – 1136Combined sources15
Beta strandi1148 – 1150Combined sources3
Beta strandi1153 – 1155Combined sources3
Beta strandi1158 – 1161Combined sources4
Helixi1169 – 1174Combined sources6
Helixi1182 – 1201Combined sources20
Helixi1211 – 1213Combined sources3
Beta strandi1214 – 1216Combined sources3
Beta strandi1222 – 1224Combined sources3
Turni1232 – 1235Combined sources4
Helixi1236 – 1239Combined sources4
Helixi1250 – 1253Combined sources4
Helixi1256 – 1259Combined sources4
Helixi1266 – 1282Combined sources17
Turni1287 – 1290Combined sources4
Helixi1293 – 1295Combined sources3
Helixi1296 – 1301Combined sources6
Helixi1314 – 1323Combined sources10
Helixi1328 – 1330Combined sources3
Helixi1334 – 1347Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PLSX-ray2.24A1060-1357[»]
4FWWX-ray1.85A42-568[»]
4QT8X-ray3.00A/B25-683[»]
ProteinModelPortaliQ04912.
SMRiQ04912.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 522SemaPROSITE-ProRule annotationAdd BLAST492
Domaini569 – 671IPT/TIG 1Add BLAST103
Domaini684 – 767IPT/TIG 2Add BLAST84
Domaini770 – 860IPT/TIG 3Add BLAST91
Domaini1082 – 1345Protein kinasePROSITE-ProRule annotationAdd BLAST264

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi306 – 309Poly-Arg4
Compositional biasi962 – 968Poly-Leu7

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

eggNOGiKOG1095. Eukaryota.
KOG3610. Eukaryota.
ENOG410XRIK. LUCA.
HOGENOMiHOG000220900.
HOVERGENiHBG104342.
InParanoidiQ04912.
KOiK05100.
OrthoDBiEOG091G0751.
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.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016201. PSI.
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. 3 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.
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. AlignAdd to basket

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
Also known as: sf-RON

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. Expressed at higher level in cancer cells.1 Publication
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)DescriptionActionsGraphical viewLength
Sequence conflicti209A → G in CAA49634 (PubMed:8386824).Curated1
Sequence conflicti813R → RQ in ACF47620 (PubMed:18593464).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04176875R → S.1 PublicationCorresponds to variant rs35887539dbSNPEnsembl.1
Natural variantiVAR_04176995P → T.1 PublicationCorresponds to variant rs55908300dbSNPEnsembl.1
Natural variantiVAR_041770185R → C.1 PublicationCorresponds to variant rs55633379dbSNPEnsembl.1
Natural variantiVAR_076928306R → H in NPCA3. 1 Publication1
Natural variantiVAR_006350322R → Q.2 PublicationsCorresponds to variant rs2230593dbSNPEnsembl.1
Natural variantiVAR_076929327A → T in NPCA3; unknown pathological significance. 1 Publication1
Natural variantiVAR_041771356G → D.1 PublicationCorresponds to variant rs35924402dbSNPEnsembl.1
Natural variantiVAR_029238434S → L.1 PublicationCorresponds to variant rs2230591dbSNPEnsembl.1
Natural variantiVAR_029239440N → S.Corresponds to variant rs2230592dbSNPEnsembl.1
Natural variantiVAR_041772465G → D.1 PublicationCorresponds to variant rs34564898dbSNPEnsembl.1
Natural variantiVAR_041773504R → C.1 PublicationCorresponds to variant rs34350470dbSNPEnsembl.1
Natural variantiVAR_041774523Q → R.2 PublicationsCorresponds to variant rs2230590dbSNPEnsembl.1
Natural variantiVAR_041775613Q → P.1 PublicationCorresponds to variant rs35986685dbSNPEnsembl.1
Natural variantiVAR_076930670V → G in NPCA3; unknown pathological significance. 1 Publication1
Natural variantiVAR_041776900V → M.1 PublicationCorresponds to variant rs56091918dbSNPEnsembl.1
Natural variantiVAR_076931973A → T in NPCA3; unknown pathological significance. 1 Publication1
Natural variantiVAR_0617491195S → G.1 PublicationCorresponds to variant rs7433231dbSNPEnsembl.1
Natural variantiVAR_0417771304R → G.1 Publication1
Natural variantiVAR_0245771335R → G.1 PublicationCorresponds to variant rs1062633dbSNPEnsembl.1
Natural variantiVAR_0417781360Y → C.1 PublicationCorresponds to variant rs56330223dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038919411 – 516Missing in isoform RON-2. 1 PublicationAdd BLAST106
Alternative sequenceiVSP_038920475 – 495ELVRS…LGDSG → GPHPHSPLALGPCLHPHFAH I in isoform RON-1. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_038921496 – 1400Missing in isoform RON-1. 1 PublicationAdd BLAST905
Alternative sequenceiVSP_038922628 – 647PVPRK…EPLGT → YNLVPPLPFPEGGNQAAPSP in isoform RON-2 and isoform RON-4. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_038923648 – 1400Missing in isoform RON-2 and isoform RON-4. 1 PublicationAdd BLAST753
Alternative sequenceiVSP_005007884 – 932Missing in isoform Delta-RON. CuratedAdd BLAST49
Alternative sequenceiVSP_038924884 – 907YIGLG…ESCQH → VSVRDRGRDSWGSESRGQPT GWSS in isoform RON-3. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_038925908 – 1400Missing in isoform RON-3. 1 PublicationAdd BLAST493

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001244937.2.
NP_002438.2. NM_002447.3.
UniGeneiHs.517973.

Genome annotation databases

EnsembliENST00000296474; ENSP00000296474; ENSG00000164078.
ENST00000344206; ENSP00000341325; ENSG00000164078.
GeneIDi4486.
KEGGihsa:4486.
UCSCiuc003cxy.5. human. [Q04912-1]

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:
EMBLi
GenBanki
DDBJi
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_001244937.2.
NP_002438.2. NM_002447.3.
UniGeneiHs.517973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PLSX-ray2.24A1060-1357[»]
4FWWX-ray1.85A42-568[»]
4QT8X-ray3.00A/B25-683[»]
ProteinModelPortaliQ04912.
SMRiQ04912.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110592. 23 interactors.
DIPiDIP-6029N.
IntActiQ04912. 15 interactors.
MINTiMINT-6539690.
STRINGi9606.ENSP00000296474.

Chemistry databases

BindingDBiQ04912.
ChEMBLiCHEMBL2689.
GuidetoPHARMACOLOGYi1816.

PTM databases

iPTMnetiQ04912.
PhosphoSitePlusiQ04912.

Polymorphism and mutation databases

BioMutaiMST1R.
DMDMi294862462.

Proteomic databases

MaxQBiQ04912.
PaxDbiQ04912.
PeptideAtlasiQ04912.
PRIDEiQ04912.

Protocols and materials databases

DNASUi4486.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296474; ENSP00000296474; ENSG00000164078.
ENST00000344206; ENSP00000341325; ENSG00000164078.
GeneIDi4486.
KEGGihsa:4486.
UCSCiuc003cxy.5. human. [Q04912-1]

Organism-specific databases

CTDi4486.
DisGeNETi4486.
GeneCardsiMST1R.
HGNCiHGNC:7381. MST1R.
HPAiCAB008972.
HPA007657.
HPA008180.
MIMi255995. phenotype.
600168. gene.
617075. phenotype.
neXtProtiNX_Q04912.
PharmGKBiPA31186.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1095. Eukaryota.
KOG3610. Eukaryota.
ENOG410XRIK. LUCA.
HOGENOMiHOG000220900.
HOVERGENiHBG104342.
InParanoidiQ04912.
KOiK05100.
OrthoDBiEOG091G0751.
PhylomeDBiQ04912.
TreeFamiTF317402.

Enzyme and pathway databases

BioCyciZFISH:HS09003-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-8852405. Signaling by MST1.
SignaLinkiQ04912.
SIGNORiQ04912.

Miscellaneous databases

ChiTaRSiMST1R. human.
GeneWikiiMST1R.
GenomeRNAii4486.
PROiQ04912.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164078.
CleanExiHS_MST1R.
ExpressionAtlasiQ04912. baseline and differential.
GenevisibleiQ04912. HS.

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.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016201. PSI.
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. 3 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.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 180 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

Similar proteinsi

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