EzCatDB: M00330
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DB codeM00330
RLCP classification3.103.130000.1162 : Transfer
CATH domainDomain 1-.-.-.-
Domain 22.60.40.10 : Immunoglobulin-like
Domain 32.60.40.10 : Immunoglobulin-like
Domain 42.60.40.10 : Immunoglobulin-like
Domain 52.60.40.10 : Immunoglobulin-like
Domain 62.60.40.10 : Immunoglobulin-like
Domain 7-.-.-.-
Domain 8-.-.-.-
Domain 93.30.200.20 : Phosphorylase Kinase; domain 1
Domain 101.10.510.10 : Transferase(Phosphotransferase); domain 1Catalytic domain
Domain 11-.-.-.-
E.C.2.7.10.1

CATH domainRelated DB codes (homologues)
1.10.510.10 : Transferase(Phosphotransferase); domain 1M00125,M00124,M00131,T00224,M00127,M00129,M00130,M00132,M00136,M00196,M00197,M00198,M00304,M00323,M00325,M00326,M00327,M00328,M00329,M00331,M00332,M00333,M00335,M00339,M00344
2.60.40.10 : Immunoglobulin-likeM00131,T00257,T00005,M00113,M00127,M00132,M00323,M00325,M00327,M00329,M00331,M00332,T00307,D00166,D00500,M00112,M00193,T00063,T00065,T00067,T00245
3.30.200.20 : Phosphorylase Kinase; domain 1M00125,M00124,M00131,T00224,M00127,M00129,M00130,M00132,M00136,M00196,M00197,M00198,M00304,M00323,M00325,M00326,M00327,M00328,M00329,M00331,M00332,M00333,M00335,M00339,M00344,D00298

Enzyme Name
UniProtKBKEGG

P09581P07333
Protein nameMacrophage colony-stimulating factor 1 receptor (CSF-1 receptor) (CSF-1-R) (CSF-1R) (M-CSF-R) (EC 2.7.10.1) (Proto-oncogene c-Fms)AltName: CD_antigen=CD115;Macrophage colony-stimulating factor 1 receptor (CSF-1 receptor) (CSF-1-R) (CSF-1R) (M-CSF-R) (EC 2.7.10.1) (Proto-oncogene c-Fms)AltName: CD_antigen=CD115;Receptor protein-tyrosine kinase
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
C-FMS
CD115
CKIT
CSF1R
KIT
Protein-tyrosine kinase (ambiguous)
Protein tyrosine kinase (ambiguous)
Receptor protein tyrosine kinase
SynonymsNoneNone
RefSeqNP_001032948.2 (Protein)
NM_001037859.2 (DNA/RNA sequence)
NP_005202.2 (Protein)
NM_005211.3 (DNA/RNA sequence)
PfamPF07679 (I-set)
PF07714 (Pkinase_Tyr)
[Graphical view]
PF00047 (ig)
PF07714 (Pkinase_Tyr)
[Graphical view]


UniProtKB:Accession NumberP09581P07333
Entry nameCSF1R_MOUSECSF1R_HUMAN
ActivityATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SubunitMonomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts with INPPL1/SHIP2 and THOC5. Interacts (tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2.Interacts with INPPL1/SHIP2 and THOC5 (By similarity). Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts (tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2.
Subcellular locationCell membrane, Single-pass type I membrane protein. Note=The autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.Cell membrane, Single-pass type I membrane protein.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00002C00585C00008C01167
CompoundMgATP[protein]-L-tyrosineADP[protein]-L-tyrosine phosphate
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotidearomatic ring (only carbon atom),peptide/proteinamine group,nucleotidearomatic ring (only carbon atom),peptide/protein,phosphate group/phosphate ion
ChEBI18420
15422

16761

PubChem888
5957

6022

             
3ejjX01UnboundUnboundUnboundUnboundUnbound
4expX01UnboundUnboundUnboundUnboundUnbound
4dkdC01UnboundUnboundUnboundUnboundUnbound
3ejjX02UnboundUnboundUnboundUnboundUnbound
4expX02UnboundUnboundUnboundUnboundUnbound
4dkdC02UnboundUnboundUnboundUnboundUnbound
3ejjX03UnboundUnboundUnboundUnboundUnbound
4expX03UnboundUnboundUnboundUnboundUnbound
4dkdC03UnboundUnboundUnboundUnboundUnbound
2i0vA01UnboundUnboundUnboundUnboundUnbound
2i0yA01UnboundUnboundUnboundUnboundUnbound
2i1mA01UnboundUnboundUnboundUnboundUnbound
2ogvA01UnboundUnboundUnboundUnboundUnbound
3beaA01UnboundUnboundUnboundUnboundUnbound
3dpkA01UnboundUnboundUnboundUnboundUnbound
3krjA01UnboundUnboundUnboundUnboundUnbound
3krlA01UnboundUnboundUnboundUnboundUnbound
3lcdA01UnboundUnboundUnboundUnboundUnbound
3lcoA01UnboundUnboundUnboundUnboundUnbound
2i0vA02UnboundUnboundUnboundUnboundUnbound
2i0yA02UnboundUnboundUnboundUnboundUnbound
2i1mA02UnboundUnboundUnboundUnboundUnbound
2ogvA02UnboundUnboundUnboundUnboundUnbound
3beaA02UnboundUnboundUnboundUnboundUnbound
3dpkA02UnboundUnboundUnboundUnboundUnbound
3krjA02UnboundUnboundUnboundUnboundUnbound
3krlA02UnboundUnboundUnboundUnboundUnbound
3lcdA02UnboundUnboundUnboundUnboundUnbound
3lcoA02UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [6], [7] & Swiss-prot;P09581, P07333
pdbCatalytic residuesCofactor-binding residues
          
3ejjX01 
 
4expX01 
 
4dkdC01 
 
3ejjX02 
 
4expX02 
 
4dkdC02 
 
3ejjX03 
 
4expX03 
 
4dkdC03 
 
2i0vA01 
 
2i0yA01 
 
2i1mA01 
 
2ogvA01 
 
3beaA01 
 
3dpkA01 
 
3krjA01 
 
3krlA01 
 
3lcdA01 
 
3lcoA01 
 
2i0vA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
2i0yA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
2i1mA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
2ogvA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
3beaA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
3dpkA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
3krjA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
3krlA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
3lcdA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)
3lcoA02ASP 778;ARG 782
ASN 783;ASP 796(Magnesium binding)


references
[1]
PubMed ID2140428
JournalMol Cell Biol
Year1990
Volume10
Pages2528-38
AuthorsTapley P, Kazlauskas A, Cooper JA, Rohrschneider LR
TitleMacrophage colony-stimulating factor-induced tyrosine phosphorylation of c-fms proteins expressed in FDC-P1 and BALB/c 3T3 cells.
[2]
PubMed ID2168557
JournalProc Natl Acad Sci U S A
Year1990
Volume87
Pages6738-42
AuthorsRoussel MF, Shurtleff SA, Downing JR, Sherr CJ
TitleA point mutation at tyrosine-809 in the human colony-stimulating factor 1 receptor impairs mitogenesis without abrogating tyrosine kinase activity, association with phosphatidylinositol 3-kinase, or induction of c-fos and junB genes.
[3]
PubMed ID1652061
JournalMol Cell Biol
Year1991
Volume11
Pages4698-709
Authorsvan der Geer P, Hunter T
TitleTyrosine 706 and 807 phosphorylation site mutants in the murine colony-stimulating factor-1 receptor are unaffected in their ability to bind or phosphorylate phosphatidylinositol-3 kinase but show differential defects in their ability to induce early response gene transcription.
[4]
PubMed ID10705574
JournalGrowth Factors
Year2000
Volume17
Pages155-66
AuthorsBourette RP, Rohrschneider LR
TitleEarly events in M-CSF receptor signaling.
[5]
PubMed ID15519852
JournalTrends Cell Biol
Year2004
Volume14
Pages628-38
AuthorsPixley FJ, Stanley ER
TitleCSF-1 regulation of the wandering macrophage: complexity in action.
[6]
PubMed ID17132624
JournalJ Biol Chem
Year2007
Volume282
Pages4094-101
AuthorsSchubert C, Schalk-Hihi C, Struble GT, Ma HC, Petrounia IP, Brandt B, Deckman IC, Patch RJ, Player MR, Spurlino JC, Springer BA
TitleCrystal structure of the tyrosine kinase domain of colony-stimulating factor-1 receptor (cFMS) in complex with two inhibitors.
Related PDB2i0v,2i0y,2i1m
Related UniProtKBP07333
[7]
PubMed ID17292918
JournalJ Mol Biol
Year2007
Volume367
Pages839-47
AuthorsWalter M, Lucet IS, Patel O, Broughton SE, Bamert R, Williams NK, Fantino E, Wilks AF, Rossjohn J
TitleThe 2.7 A crystal structure of the autoinhibited human c-Fms kinase domain.
Related PDB2ogv
Related UniProtKBP07333
[8]
PubMed ID18342505
JournalBioorg Med Chem Lett
Year2008
Volume18
Pages2355-61
AuthorsHuang H, Hutta DA, Hu H, DesJarlais RL, Schubert C, Petrounia IP, Chaikin MA, Manthey CL, Player MR
TitleDesign and synthesis of a pyrido[2,3-d]pyrimidin-5-one class of anti-inflammatory FMS inhibitors.
Related PDB3bea
Related UniProtKBP07333
[9]
PubMed ID19017797
JournalProc Natl Acad Sci U S A
Year2008
Volume105
Pages18267-72
AuthorsChen X, Liu H, Focia PJ, Shim AH, He X
TitleStructure of macrophage colony stimulating factor bound to FMS: diverse signaling assemblies of class III receptor tyrosine kinases.
Related PDB3ejj
Related UniProtKBP09581
[10]
PubMed ID19193011
JournalJ Med Chem
Year2009
Volume52
Pages1081-99
AuthorsHuang H, Hutta DA, Rinker JM, Hu H, Parsons WH, Schubert C, DesJarlais RL, Crysler CS, Chaikin MA, Donatelli RR, Chen Y, Cheng D, Zhou Z, Yurkow E, Manthey CL, Player MR
TitlePyrido[2,3-d]pyrimidin-5-ones: a novel class of antiinflammatory macrophage colony-stimulating factor-1 receptor inhibitors.
Related PDB3dpk
Related UniProtKBP07333
[11]
PubMed ID20137931
JournalBioorg Med Chem Lett
Year2010
Volume20
Pages1543-7
AuthorsMeyers MJ, Pelc M, Kamtekar S, Day J, Poda GI, Hall MK, Michener ML, Reitz BA, Mathis KJ, Pierce BS, Parikh MD, Mischke DA, Long SA, Parlow JJ, Anderson DR, Thorarensen A
TitleStructure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode.
Related PDB3lcd,3lco
Related UniProtKBP07333

comments
This enzyme belongs to platelet-derived growth factor (PDGF) receptor family (see [6]), along with homologous enzymes, such as Receptor-type tyrosine-protein kinase FLT3 (M00331 in EzCatDB) and Tyrosine-protein kinase Kit (M00323 in EzCatDB). This enzyme seems to interact with different proteins from those proteins which are interacted with the homologous enzymes.
The catalytic domain of this enzyme is homologous to that of vascular endothelial growth factor receptor (M00131 in EzCatDB).

createdupdated
2011-11-172012-12-05


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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