EzCatDB: M00331
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00331
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,M00330,M00332,M00333,M00335,M00339,M00344
2.60.40.10 : Immunoglobulin-likeM00131,T00257,T00005,M00113,M00127,M00132,M00323,M00325,M00327,M00329,M00330,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,M00330,M00332,M00333,M00335,M00339,M00344,D00298

Enzyme Name
UniProtKBKEGG

P36888
Protein nameReceptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase-2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Stem cell tyrosine kinase 1) (STK-1)AltName: CD_antigen=CD135;Receptor protein-tyrosine kinase
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
CD135
CDw135
FLK1
FLK2
FLT1
FLT2
FLT3
FLT4
FMS
Fv2
Protein-tyrosine kinase (ambiguous)
Protein tyrosine kinase (ambiguous)
Receptor protein tyrosine kinase
STK
STK1
SynonymsNone
RefSeqNP_004110.2 (Protein)
NM_004119.2 (DNA/RNA sequence)
PfamPF00047 (ig)
PF07714 (Pkinase_Tyr)
[Graphical view]


UniProtKB:Accession NumberP36888
Entry nameFLT3_HUMAN
ActivityATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SubunitMonomer in the absence of bound FLT3LG. Homodimer in the presence of bound FLT3LG. Interacts with FIZ1 following ligand activation (By similarity). Interacts with FES, FER, LYN, FGR, HCK, SRC and GRB2. Interacts with PTPRJ/DEP-1 and PTPN11/SHP2.
Subcellular locationMembrane, Single-pass type I membrane protein. Endoplasmic reticulum lumen. Note=Constitutively activated mutant forms with internal tandem duplications are less efficiently transported to the cell surface and a significant proportion is retained in an immature form in the endoplasmic reticulum lumen. The activated kinase is rapidly targeted for degradation.
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

             
3qs7E01UnboundUnboundUnboundUnboundUnbound
3qs7F01UnboundUnboundUnboundUnboundUnbound
3qs9E01UnboundUnboundUnboundUnboundUnbound
3qs9G01UnboundUnboundUnboundUnboundUnbound
3qs9H01UnboundUnboundUnboundUnboundUnbound
3qs7E02UnboundUnboundUnboundUnboundUnbound
3qs7F02UnboundUnboundUnboundUnboundUnbound
3qs7G01UnboundUnboundUnboundUnboundUnbound
3qs7H01UnboundUnboundUnboundUnboundUnbound
3qs9E02UnboundUnboundUnboundUnboundUnbound
3qs9G02UnboundUnboundUnboundUnboundUnbound
3qs9H02UnboundUnboundUnboundUnboundUnbound
3qs9F01UnboundUnboundUnboundUnboundUnbound
3qs7E03UnboundUnboundUnboundUnboundUnbound
3qs7F03UnboundUnboundUnboundUnboundUnbound
3qs7G02UnboundUnboundUnboundUnboundUnbound
3qs7H02UnboundUnboundUnboundUnboundUnbound
3qs9E03UnboundUnboundUnboundUnboundUnbound
3qs9G03UnboundUnboundUnboundUnboundUnbound
3qs9H03UnboundUnboundUnboundUnboundUnbound
3qs9F02UnboundUnboundUnboundUnboundUnbound
3qs7E04UnboundUnboundUnboundUnboundUnbound
3qs7F04UnboundUnboundUnboundUnboundUnbound
3qs7H03UnboundUnboundUnboundUnboundUnbound
3qs9E04UnboundUnboundUnboundUnboundUnbound
3qs9G04UnboundUnboundUnboundUnboundUnbound
3qs9H04UnboundUnboundUnboundUnboundUnbound
3qs9F03UnboundUnboundUnboundUnboundUnbound
3qs9E05UnboundUnboundUnboundUnboundUnbound
3qs9G05UnboundUnboundUnboundUnboundUnbound
3qs9H05UnboundUnboundUnboundUnboundUnbound
3qs9F04UnboundUnboundUnboundUnboundUnbound
1rjbA01UnboundUnboundUnboundUnboundUnbound
1rjbA02UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [2] & Swiss-prot;P36888
pdbCatalytic residuesCofactor-binding residues
          
3qs7E01 
 
3qs7F01 
 
3qs9E01 
 
3qs9G01 
 
3qs9H01 
 
3qs7E02 
 
3qs7F02 
 
3qs7G01 
 
3qs7H01 
 
3qs9E02 
 
3qs9G02 
 
3qs9H02 
 
3qs9F01 
 
3qs7E03 
 
3qs7F03 
 
3qs7G02 
 
3qs7H02 
 
3qs9E03 
 
3qs9G03 
 
3qs9H03 
 
3qs9F02 
 
3qs7E04 
 
3qs7F04 
 
3qs7H03 
 
3qs9E04 
 
3qs9G04 
 
3qs9H04 
 
3qs9F03 
 
3qs9E05 
 
3qs9G05 
 
3qs9H05 
 
3qs9F04 
 
1rjbA01 
 
1rjbA02ASP 811;ARG 815
ASN 816;ASP 829(Magnesium binding)


references
[1]
PubMed ID10881197
JournalNat Struct Biol
Year2000
Volume7
Pages486-91
AuthorsSavvides SN, Boone T, Andrew Karplus P
TitleFlt3 ligand structure and unexpected commonalities of helical bundles and cystine knots.
[2]
PubMed ID14759363
JournalMol Cell
Year2004
Volume13
Pages169-78
AuthorsGriffith J, Black J, Faerman C, Swenson L, Wynn M, Lu F, Lippke J, Saxena K
TitleThe structural basis for autoinhibition of FLT3 by the juxtamembrane domain.
Related PDB1rjb
Related UniProtKBP36888
[3]
PubMed ID18628457
JournalClin Cancer Res
Year2008
Volume14
Pages4437-45
AuthorsVempati S, Reindl C, Wolf U, Kern R, Petropoulos K, Naidu VM, Buske C, Hiddemann W, Kohl TM, Spiekermann K
TitleTransformation by oncogenic mutants and ligand-dependent activation of FLT3 wild-type requires the tyrosine residues 589 and 591.
[4]
PubMed ID21389326
JournalBlood
Year2011
Volume118
Pages60-8
AuthorsVerstraete K, Vandriessche G, Januar M, Elegheert J, Shkumatov AV, Desfosses A, Van Craenenbroeck K, Svergun DI, Gutsche I, Vergauwen B, Savvides SN
TitleStructural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
Related PDB3qs7,3qs9
Related UniProtKBP36888

comments
This enzyme belongs to platelet-derived growth factor (PDGF) receptor family, along with homologous enzymes, such as colony-stimulating factor-1 receptor (CSF-1-R, cFMS) (M00330 in EzCatDB) and tyrosine-protein kinase Kit (Kit) (M00323 in EzCatDB).
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
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
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 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.