FLT3_MOUSE - dbPTM
FLT3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLT3_MOUSE
UniProt AC Q00342
Protein Name Receptor-type tyrosine-protein kinase FLT3
Gene Name Flt3
Organism Mus musculus (Mouse).
Sequence Length 1000
Subcellular Localization Membrane
Single-pass type I membrane protein. Endoplasmic reticulum lumen. Constitutively activated mutant forms with internal tandem duplications are less efficiently transported to the cell surface and a significant proportion is retained in an im
Protein Description Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways..
Protein Sequence MRALAQRSDRRLLLLVVLSVMILETVTNQDLPVIKCVLISHENNGSSAGKPSSYRMVRGSPEDLQCTPRRQSEGTVYEAATVEVAESGSITLQVQLATPGDLSCLWVFKHSSLGCQPHFDLQNRGIVSMAILNVTETQAGEYLLHIQSEAANYTVLFTVNVRDTQLYVLRRPYFRKMENQDALLCISEGVPEPTVEWVLCSSHRESCKEEGPAVVRKEEKVLHELFGTDIRCCARNALGRESTKLFTIDLNQAPQSTLPQLFLKVGEPLWIRCKAIHVNHGFGLTWELEDKALEEGSYFEMSTYSTNRTMIRILLAFVSSVGRNDTGYYTCSSSKHPSQSALVTILEKGFINATSSQEEYEIDPYEKFCFSVRFKAYPRIRCTWIFSQASFPCEQRGLEDGYSISKFCDHKNKPGEYIFYAENDDAQFTKMFTLNIRKKPQVLANASASQASCSSDGYPLPSWTWKKCSDKSPNCTEEIPEGVWNKKANRKVFGQWVSSSTLNMSEAGKGLLVKCCAYNSMGTSCETIFLNSPGPFPFIQDNISFYATIGLCLPFIVVLIVLICHKYKKQFRYESQLQMIQVTGPLDNEYFYVDFRDYEYDLKWEFPRENLEFGKVLGSGAFGRVMNATAYGISKTGVSIQVAVKMLKEKADSCEKEALMSELKMMTHLGHHDNIVNLLGACTLSGPVYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQAHSNSSMPGSREVQLHPPLDQLSGFNGNSIHSEDEIEYENQKRLAEEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDILSDSSYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQSGFKMEQPFYATEGIYFVMQSCWAFDSRKRPSFPNLTSFLGCQLAEAEEAMYQNMGGNVPEHPSIYQNRRPLSREAGSEPPSPQAQVKIHRERS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Methylation------MRALAQRSD
------CCHHHHHCH
38.00-
7Methylation-MRALAQRSDRRLLL
-CCHHHHHCHHHHHH
34.61-
19PhosphorylationLLLLVVLSVMILETV
HHHHHHHHHHHHHHC
9.68-
25PhosphorylationLSVMILETVTNQDLP
HHHHHHHHCCCCCCC
29.23-
27PhosphorylationVMILETVTNQDLPVI
HHHHHHCCCCCCCEE
34.28-
44N-linked_GlycosylationVLISHENNGSSAGKP
EEEEECCCCCCCCCC
49.06-
133N-linked_GlycosylationIVSMAILNVTETQAG
EEEEEEEEECCCCCC
32.33-
152N-linked_GlycosylationHIQSEAANYTVLFTV
EEEECCCCEEEEEEE
38.95-
164PhosphorylationFTVNVRDTQLYVLRR
EEEECCCCEEEEEEC
15.2020139300
307N-linked_GlycosylationEMSTYSTNRTMIRIL
EEECCCCCHHHHHHH
31.33-
324N-linked_GlycosylationFVSSVGRNDTGYYTC
HHHHCCCCCCCEEEC
45.31-
352N-linked_GlycosylationILEKGFINATSSQEE
HHHHCCCCCCCCCCE
34.60-
445N-linked_GlycosylationKKPQVLANASASQAS
CCCEEEECCCCCHHC
30.21-
474N-linked_GlycosylationKCSDKSPNCTEEIPE
ECCCCCCCCCCCCCC
53.05-
500PhosphorylationFGQWVSSSTLNMSEA
HCEEECCCCCCCCCC
29.4328059163
503N-linked_GlycosylationWVSSSTLNMSEAGKG
EECCCCCCCCCCCCC
31.83-
542N-linked_GlycosylationPFPFIQDNISFYATI
CCCCCCCCHHHHHHH
18.54-
573PhosphorylationKYKKQFRYESQLQMI
HHHHHCCCHHHCEEE
22.63-
575PhosphorylationKKQFRYESQLQMIQV
HHHCCCHHHCEEEEE
27.53-
590PhosphorylationTGPLDNEYFYVDFRD
ECCCCCCEEEEECCC
13.3821262971
592PhosphorylationPLDNEYFYVDFRDYE
CCCCCEEEEECCCCE
9.7522817900
600PhosphorylationVDFRDYEYDLKWEFP
EECCCCEEEECEECC
21.9821262971
631PhosphorylationRVMNATAYGISKTGV
HHHEEEECCCCCCCC
15.61-
727PhosphorylationKEHNFSFYPTFQAHS
HHCCCCCCCEEECCC
12.70-
729PhosphorylationHNFSFYPTFQAHSNS
CCCCCCCEEECCCCC
21.83-
760PhosphorylationLSGFNGNSIHSEDEI
CCCCCCCCCCCHHHH
24.07-
769PhosphorylationHSEDEIEYENQKRLA
CCHHHHHHHHHHHHH
26.33-
796PhosphorylationEDLLCFAYQVAKGME
HHHHHHHHHHHCCCC
5.35-
831GlutathionylationHGKVVKICDFGLARD
CCCEEEECCCCCCHH
2.6924333276
845PhosphorylationDILSDSSYVVRGNAR
HHHCCCCEEEECCCC
13.6022817900
868PhosphorylationESLFEGIYTIKSDVW
HHHHCCEEEECHHHH
17.17-
892PhosphorylationFSLGVNPYPGIPVDA
HHCCCCCCCCCCCCH
14.6422817900
922PhosphorylationFYATEGIYFVMQSCW
EEECCCEEEEEEHHH
10.8522817900
927PhosphorylationGIYFVMQSCWAFDSR
CEEEEEEHHHHCCCC
8.11-
958PhosphorylationAEAEEAMYQNMGGNV
HHHHHHHHHHCCCCC
7.49-
972PhosphorylationVPEHPSIYQNRRPLS
CCCCHHHHCCCCCCC
44.95-
984PhosphorylationPLSREAGSEPPSPQA
CCCCCCCCCCCCHHH
35.2922817900
988PhosphorylationEAGSEPPSPQAQVKI
CCCCCCCCHHHCCEE
21.6022817900
1000PhosphorylationVKIHRERS-------
CEEECCCC-------
-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
592YPhosphorylationKinaseFLT3Q00342
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLT3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FLT3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOCS6_MOUSESocs6physical
22952242
SOCS2_MOUSESocs2physical
23548639

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLT3_MOUSE

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Related Literatures of Post-Translational Modification

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